Trans-3-hydroxy-L-proline dehydratase

Details

Name
Trans-3-hydroxy-L-proline dehydratase
Synonyms
  • 4.2.1.77
  • C14orf149
  • Trans-L-3-hydroxyproline dehydratase
Gene Name
L3HYPDH
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016757|Trans-3-hydroxy-L-proline dehydratase
MESALAVPRLPPHDPGTPVLSVVDMHTGGEPLRIVLAGCPEVSGPTLLAKRRYMRQHLDH
VRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGL
VPAPPAGTREARVNIHCPCGLVTAFVACEDGRSHGPVRFHSVPAFVLATDLMVDVPGHGK
VMVDIAYGGAFYAFVTAEKLGLDICSAKTRDLVDAASAVTEAVKAQFKINHPDSEDLAFL
YGTILTDGKDAYTKEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQMRAFKS
SATGSVFTGKAVREAKCGDFKAVIVEVSGQAHYTGTASFIIEDDDPLRDGFLLK
Number of residues
354
Molecular Weight
38137.395
Theoretical pI
6.56
GO Classification
Functions
hydro-lyase activity / trans-L-3-hydroxyproline dehydratase activity
Processes
metabolic process
General Function
Trans-l-3-hydroxyproline dehydratase activity
Specific Function
Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016758|Trans-3-hydroxy-L-proline dehydratase (L3HYPDH)
ATGGAGAGCGCGCTGGCGGTGCCCCGGCTGCCCCCGCATGATCCAGGGACGCCGGTGCTG
TCGGTGGTGGACATGCACACGGGCGGCGAGCCCTTGCGTATCGTGCTGGCGGGGTGTCCG
GAGGTGTCTGGGCCCACCCTGCTGGCCAAGCGGCGCTACATGCGCCAGCACCTTGACCAC
GTGCGGCGACGGCTCATGTTCGAGCCCCGAGGGCACCGGGACATGTACGGGGCGGTCCTA
GTCCCGAGCGAGCTGCCGGACGCGCATCTGGGCGTCCTGTTCCTGCACAACGAGGGCTAC
AGCTCCATGTGCGGCCACGCAGTGCTGGCGCTGGGCCGCTTCGCTTTGGACTTCGGGCTT
GTGCCGGCGCCCCCTGCGGGCACCCGCGAGGCCCGCGTCAATATCCACTGCCCCTGCGGG
CTGGTGACCGCCTTCGTGGCATGCGAGGACGGCCGCAGCCACGGACCGGTGCGCTTCCAC
AGCGTCCCGGCCTTCGTGCTGGCCACAGATCTCATGGTGGATGTTCCTGGACATGGAAAG
GTGATGGTGGACATTGCATATGGCGGTGCATTTTATGCATTTGTTACTGCTGAAAAGTTA
GGACTAGACATTTGTTCTGCAAAGACCAGGGACCTTGTGGATGCAGCGAGTGCAGTGACA
GAGGCAGTGAAAGCTCAGTTTAAAATTAATCATCCTGATAGTGAAGACCTTGCCTTTTTA
TATGGAACTATATTAACAGATGGAAAAGATGCTTATACCAAGGAACCAACCACCAACATT
TGTGTTTTTGCAGATGAACAGGTTGACAGAAGTCCCACTGGCTCAGGAGTGACAGCCCGA
ATTGCCTTACAGTATCACAAAGGGCTTCTGGAACTGAACCAGATGAGAGCCTTCAAAAGC
AGTGCAACTGGCTCAGTATTCACAGGGAAAGCTGTGAGGGAAGCGAAATGTGGTGATTTT
AAAGCTGTTATAGTGGAAGTATCAGGACAAGCCCATTACACGGGTACAGCAAGCTTTATA
ATAGAAGATGACGACCCATTGAGGGATGGATTTCTTCTCAAGTGA
Chromosome Location
14
Locus
14q23.1
External Identifiers
ResourceLink
UniProtKB IDQ96EM0
UniProtKB Entry NameT3HPD_HUMAN
GenBank Protein ID15082426
GenBank Gene IDBC012131
GenAtlas IDC14orf149
HGNC IDHGNC:20488
General References
  1. 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]
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  3. 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]
  4. 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]
  5. Visser WF, Verhoeven-Duif NM, de Koning TJ: Identification of a human trans-3-hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes. J Biol Chem. 2012 Jun 22;287(26):21654-62. doi: 10.1074/jbc.M112.363218. Epub 2012 Apr 23. [Article]
  6. Watanabe S, Tanimoto Y, Yamauchi S, Tozawa Y, Sawayama S, Watanabe Y: Identification and characterization of trans-3-hydroxy-l-proline dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria. FEBS Open Bio. 2014 Feb 26;4:240-50. doi: 10.1016/j.fob.2014.02.010. eCollection 2014. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00172ProlinenutraceuticalunknownDetails