Protocatechuate 3,4-dioxygenase alpha chain

Details

Name
Protocatechuate 3,4-dioxygenase alpha chain
Synonyms
  • 1.13.11.3
  • 3,4-PCD
Gene Name
pcaG
Organism
Pseudomonas putida
Amino acid sequence
>lcl|BSEQ0017310|Protocatechuate 3,4-dioxygenase alpha chain
MPIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLAKPDAPGEHILLLGQVYDGN
GHLVRDSFLEVWQADANGEYQDAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAG
VPMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNLIEQPQRRETLIAKRCEVDG
KTAYRFDIRIQGEGETVFFDF
Number of residues
201
Molecular Weight
22386.9
Theoretical pI
4.77
GO Classification
Functions
ferric iron binding / protocatechuate 3,4-dioxygenase activity
Processes
beta-ketoadipate pathway
General Function
Protocatechuate 3,4-dioxygenase activity
Specific Function
Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0007711|720 bp
ATGCCCGCCCAGGACAACAGCCGCTTCGTGATCCGTGATCGCAACTGGCACCCCAAAGCC
CTTACGCCTGACTACAAAACGTCCATTGCCCGCTCGCCGCGCCAGGCACTGGTCAGCATT
CCACAGTCGATCAGCGAAACCACTGGTCCGAACTTTTCCCACCTGGGCTTCGGCGCCCAC
GACCATGACCTGCTGCTGAACTTCAACAACGGTGGCCTGCCAATCGGCGAGCGCATCATC
GTGGCCGGCCGCGTCGTCGACCAGTACGGCAAGCCTGTGCCGAACACCCTGGTGGAGATG
TGGCAAGCCAACGCCGGTGGCCGCTACCGGCACAAGAACGACCGTTACCTGGCACCGCTG
GACCCGAACTTTGGTGGTGTCGGCCGTTGCCTGACCGACAGCGACGGCTACTACAGCTTC
CGCACCATCAAGCCGGGCCCGTACCCCTGGCGCAACGGCCCGAACGACTGGCGCCCGGCG
CACATCCACTTCGGCATCAGCGGCCCGTCGATTGCGACCAAGCTGATCACCCAGTTGTAT
TTCGAGGGTGACCCGCTGATCCCGATGTGCCCGATCGTCAAGTCGATCGCCAACCCTGAA
GCTGTACAGCAGTTGATCGCCAAGCTCGACATGAACAACGCCAACCCGATGGACTGCCTG
GCCTACCGCTTTGACATCGTGCTGCGCGGCCAGCGCAAGACCCACTTCGAAAACTGCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00436
UniProtKB Entry NamePCXA_PSEPU
GenBank Protein ID294344
GenBank Gene IDL14836
General References
  1. Frazee RW, Livingston DM, LaPorte DC, Lipscomb JD: Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes. J Bacteriol. 1993 Oct;175(19):6194-202. [Article]
  2. Kohlmiller NA, Howard JB: The primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase. II. Isolation and sequence of overlap peptides and complete sequence. J Biol Chem. 1979 Aug 10;254(15):7309-15. [Article]
  3. Ohlendorf DH, Lipscomb JD, Weber PC: Structure and assembly of protocatechuate 3,4-dioxygenase. Nature. 1988 Nov 24;336(6197):403-5. [Article]
  4. Ohlendorf DH, Orville AM, Lipscomb JD: Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution. J Mol Biol. 1994 Dec 16;244(5):586-608. [Article]
  5. Orville AM, Elango N, Lipscomb JD, Ohlendorf DH: Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site. Biochemistry. 1997 Aug 19;36(33):10039-51. [Article]
  6. Orville AM, Lipscomb JD, Ohlendorf DH: Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding. Biochemistry. 1997 Aug 19;36(33):10052-66. [Article]
  7. Elgren TE, Orville AM, Kelly KA, Lipscomb JD, Ohlendorf DH, Que L Jr: Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate. Biochemistry. 1997 Sep 23;36(38):11504-13. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB017022-(3,4-Dihydroxyphenyl)Acetic AcidexperimentalunknownDetails