Pyruvate carboxylase, mitochondrial

Details

Name
Pyruvate carboxylase, mitochondrial
Synonyms
  • 6.4.1.1
  • PCB
  • Pyruvic carboxylase
Gene Name
PC
Organism
Humans
Amino acid sequence
>lcl|BSEQ0001392|Pyruvate carboxylase, mitochondrial
MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELG
IRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGF
LSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEA
HEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIE
KPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAK
QVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDL
GLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISP
HYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQF
IDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAG
FRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSK
LFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVF
KFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSL
QYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGV
AAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEG
ARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQM
LGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFP
EPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF
KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFEL
NGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVL
SAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE
Number of residues
1178
Molecular Weight
129632.565
Theoretical pI
6.83
GO Classification
Functions
ATP binding / biotin binding / biotin carboxylase activity / DNA binding / metal ion binding / pyruvate carboxylase activity
Processes
biotin metabolic process / carbohydrate metabolic process / gluconeogenesis / glucose metabolic process / lipid metabolic process / negative regulation of gene expression / positive regulation by host of viral process / positive regulation by host of viral release from host cell / pyruvate metabolic process / small molecule metabolic process / viral RNA genome packaging / vitamin metabolic process / water-soluble vitamin metabolic process
Components
cytoplasm / cytosol / mitochondrial matrix / mitochondrion
General Function
Pyruvate carboxylase activity
Specific Function
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion matrix
Gene sequence
>lcl|BSEQ0018996|Pyruvate carboxylase, mitochondrial (PC)
ATGCTGAAGTTCCGAACAGTCCATGGGGGCCTGAGGCTCCTGGGAATCCGCCGAACCTCC
ACCGCCCCCGCTGCCTCCCCAAATGTCCGGCGCCTGGAGTATAAGCCCATCAAGAAAGTC
ATGGTGGCCAACAGAGGTGAGATTGCCATCCGTGTGTTCCGGGCCTGCACGGAGCTGGGC
ATCCGCACCGTAGCCATCTACTCTGAGCAGGACACGGGCCAGATGCACCGGCAGAAAGCA
GATGAAGCCTATCTCATCGGCCGCGGCCTGGCCCCCGTGCAGGCCTACCTGCACATCCCA
GACATCATCAAGGTGGCCAAGGAGAACAACGTAGATGCAGTGCACCCTGGCTACGGGTTC
CTCTCTGAGCGAGCGGACTTCGCCCAGGCCTGCCAGGATGCAGGGGTCCGGTTTATTGGG
CCAAGCCCAGAAGTGGTCCGCAAGATGGGAGACAAGGTGGAGGCCCGGGCCATCGCCATT
GCTGCGGGTGTTCCCGTTGTCCCTGGCACAGATGCCCCCATCACGTCCCTGCATGAGGCC
CACGAGTTCTCCAACACCTACGGCTTCCCCATCATCTTCAAGGCGGCCTATGGGGGTGGA
GGGCGTGGCATGAGGGTGGTGCACAGCTACGAGGAGCTGGAGGAGAATTACACCCGGGCC
TACTCAGAGGCTCTGGCCGCCTTTGGGAATGGGGCGCTGTTTGTGGAGAAGTTCATCGAG
AAGCCACGGCACATCGAGGTGCAGATCTTGGGGGACCAGTATGGGAACATCCTGCACCTG
TACGAGCGAGACTGCTCCATCCAGCGGCGGCACCAGAAGGTGGTCGAGATTGCCCCCGCC
GCCCACCTGGACCCGCAGCTTCGGACTCGGCTCACCAGCGACTCTGTGAAACTCGCTAAA
CAGGTGGGCTACGAGAACGCAGGCACCGTGGAGTTCCTGGTGGACAGGCACGGCAAGCAC
TACTTCATCGAGGTCAACTCCCGCCTGCAGGTGGAGCACACGGTCACAGAGGAGATCACC
GACGTAGACCTGGTCCATGCTCAGATCCACGTGGCTGAGGGCAGGAGCCTACCCGACCTG
GGCCTGCGGCAGGAGAACATCCGCATCAACGGGTGTGCCATCCAGTGCCGGGTCACCACC
GAGGACCCCGCGCGCAGCTTCCAGCCGGACACCGGCCGCATTGAGGTGTTCCGGAGCGGA
GAGGGCATGGGCATCCGCCTGGATAATGCTTCCGCCTTCCAAGGAGCCGTCATCTCGCCC
CACTACGACTCCCTGCTGGTCAAAGTCATTGCCCACGGCAAAGACCACCCCACGGCCGCC
ACCAAGATGAGCAGGGCCCTTGCGGAGTTCCGCGTCCGAGGTGTGAAGACCAACATCGCC
TTCCTGCAGAATGTGCTCAACAACCAGCAGTTCCTGGCAGGCACTGTGGACACCCAGTTC
ATCGACGAGAACCCAGAGCTGTTCCAGCTGCGGCCTGCACAGAACCGGGCCCAAAAGCTG
TTGCACTACCTCGGCCATGTCATGGTAAACGGTCCAACCACCCCGATTCCCGTCAAGGCC
AGCCCCAGCCCCACGGACCCCGTTGTCCCTGCAGTGCCCATAGGCCCGCCCCCGGCTGGT
TTCAGAGACATCCTGCTGCGAGAGGGGCCTGAGGGCTTTGCTCGAGCTGTGCGGAACCAC
CCGGGGCTGCTGCTGATGGACACGACCTTCAGGGACGCCCACCAGTCACTGCTGGCCACT
CGTGTGCGCACCCACGATCTCAAAAAGATCGCCCCCTATGTTGCCCACAACTTCAGCAAG
CTCTTCAGCATGGAGAACTGGGGAGGAGCCACGTTTGACGTCGCCATGCGCTTCCTGTAT
GAGTGCCCCTGGCGGCGGCTGCAGGAGCTCCGGGAGCTCATCCCCAACATCCCTTTCCAG
ATGCTGCTGCGGGGGGCCAATGCTGTGGGCTACACCAACTACCCAGACAACGTGGTCTTC
AAGTTCTGTGAAGTGGCCAAAGAGAATGGCATGGATGTCTTCCGTGTGTTTGACTCCCTC
AACTACTTGCCCAACATGCTGCTGGGCATGGAGGCGGCAGGAAGTGCCGGAGGCGTGGTG
GAGGCTGCCATCTCATACACGGGCGACGTGGCCGACCCCAGCCGCACCAAGTACTCACTG
CAGTACTACATGGGCTTGGCCGAAGAGCTGGTGCGAGCTGGCACCCACATCCTGTGCATC
AAGGACATGGCCGGGCTGCTGAAGCCCACGGCCTGCACCATGCTGGTCAGCTCCCTCCGG
GACCGCTTCCCCGACCTCCCACTGCACATCCACACCCACGACACGTCAGGGGCAGGCGTG
GCAGCCATGCTGGCCTGTGCCCAGGCTGGAGCTGATGTGGTGGATGTGGCAGCTGATTCC
ATGTCTGGGATGACTTCACAGCCCAGCATGGGGGCCCTGGTGGCCTGTACCAGAGGGACT
CCCCTGGACACAGAGGTGCCCATGGAGCGCGTGTTTGACTACAGTGAGTACTGGGAGGGG
GCTCGGGGACTGTACGCGGCCTTCGACTGCACGGCCACCATGAAGTCTGGCAACTCGGAC
GTGTATGAAAATGAGATCCCAGGGGGCCAGTACACCAACCTGCACTTCCAGGCCCACAGC
ATGGGGCTTGGCTCCAAGTTCAAGGAGGTCAAGAAGGCCTATGTGGAGGCCAACCAGATG
CTGGGCGATCTCATCAAGGTGACGCCCTCCTCCAAGATCGTGGGGGACCTGGCCCAGTTT
ATGGTGCAGAATGGATTGAGCCGGGCAGAGGCCGAAGCTCAGGCGGAAGAGCTGTCCTTT
CCCCGCTCCGTGGTGGAGTTCCTGCAGGGCTACATCGGTGTCCCCCATGGGGGGTTCCCC
GAACCCTTTCGCTCTAAGGTACTGAAGGACCTGCCAAGGGTGGAGGGGCGGCCTGGAGCC
TCCCTCCCTCCCCTGGATCTGCAGGCACTGGAGAAGGAGCTGGTAGACCGGCATGGGGAG
GAGGTGACGCCGGAAGATGTGCTCTCAGCAGCTATGTACCCCGATGTGTTTGCCCACTTC
AAGGACTTCACTGCCACCTTTGGCCCCCTGGATAGCCTGAATACTCGCCTCTTCCTGCAG
GGACCCAAGATCGCAGAGGAGTTTGAGGTGGAGCTGGAGCGGGGCAAGACGCTGCACATC
AAAGCCCTGGCCGTGAGCGACCTGAACCGGGCCGGCCAGAGGCAGGTCTTCTTTGAGCTC
AATGGGCAGCTGCGGTCCATCTTGGTCAAGGACACCCAGGCCATGAAGGAGATGCACTTC
CACCCCAAGGCCCTAAAGGACGTGAAGGGCCAGATCGGGGCGCCCATGCCTGGGAAGGTG
ATAGACATCAAAGTGGTGGCAGGGGCCAAGGTGGCCAAGGGCCAGCCCCTGTGTGTGCTC
AGTGCCATGAAGATGGAGACTGTGGTGACCTCACCCATGGAGGGTACTGTCCGCAAGGTT
CATGTGACCAAGGACATGACACTGGAAGGTGACGACCTCATCCTGGAGATCGAGTGA
Chromosome Location
11
Locus
11q13.4-q13.5
External Identifiers
ResourceLink
UniProtKB IDP11498
UniProtKB Entry NamePYC_HUMAN
GenBank Protein ID458236
GenBank Gene IDU04641
GenAtlas IDPC
HGNC IDHGNC:8636
General References
  1. Wexler ID, Du Y, Lisgaris MV, Mandal SK, Freytag SO, Yang BS, Liu TC, Kwon M, Patel MS, Kerr DS: Primary amino acid sequence and structure of human pyruvate carboxylase. Biochim Biophys Acta. 1994 Oct 21;1227(1-2):46-52. [Article]
  2. MacKay N, Rigat B, Douglas C, Chen HS, Robinson BH: cDNA cloning of human kidney pyruvate carboxylase. Biochem Biophys Res Commun. 1994 Jul 29;202(2):1009-14. [Article]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  4. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [Article]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [Article]
  7. Freytag SO, Collier KJ: Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J Biol Chem. 1984 Oct 25;259(20):12831-7. [Article]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
  9. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  10. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  11. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  12. Xiang S, Tong L: Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction. Nat Struct Mol Biol. 2008 Mar;15(3):295-302. doi: 10.1038/nsmb.1393. Epub 2008 Feb 24. [Article]
  13. Carbone MA, MacKay N, Ling M, Cole DE, Douglas C, Rigat B, Feigenbaum A, Clarke JT, Haworth JC, Greenberg CR, Seargeant L, Robinson BH: Amerindian pyruvate carboxylase deficiency is associated with two distinct missense mutations. Am J Hum Genet. 1998 Jun;62(6):1312-9. [Article]
  14. Wexler ID, Kerr DS, Du Y, Kaung MM, Stephenson W, Lusk MM, Wappner RS, Higgins JJ: Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families. Pediatr Res. 1998 May;43(5):579-84. [Article]
  15. Monnot S, Serre V, Chadefaux-Vekemans B, Aupetit J, Romano S, De Lonlay P, Rival JM, Munnich A, Steffann J, Bonnefont JP: Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency. Hum Mutat. 2009 May;30(5):734-40. doi: 10.1002/humu.20908. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00121Biotinapproved, investigational, nutraceuticalunknowncofactorDetails
DB00119Pyruvic acidapproved, investigational, nutraceuticalunknownDetails
DB074975-(hexahydro-2-oxo-1H-thieno[3,4-D]imidazol-6-yl)pentanalexperimentalunknownDetails