Protocatechuate 3,4-dioxygenase alpha chain

Details

Name
Protocatechuate 3,4-dioxygenase alpha chain
Kind
protein
Synonyms
  • 1.13.11.3
  • 3,4-PCD
Gene Name
pcaG
UniProtKB Entry
P00436Swiss-Prot
Organism
Pseudomonas putida
NCBI Taxonomy ID
303
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
Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Specific Function
ferric iron binding
Pfam Domain Function
Signal Regions
Not Available
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
PDB ID(s)1YKK, 1YKL, 1YKM, 1YKN, 1YKO, 1YKP, 2PCD, 3LKT, 3LMX, 3LXV, 3MFL, 3MI1, 3MI5, 3MV4, 3MV6, 3PCA, 3PCB, 3PCC, 3PCD, 3PCE, 3PCF, 3PCG, 3PCH, 3PCI, 3PCJ, 3PCK, 3PCL, 3PCM, 3PCN, 3T63, 3T67, 4WHO, 4WHP, 4WHQ, 4WHR, 4WHS
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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
2-(3,4-Dihydroxyphenyl)Acetic AcidexperimentalunknowntargetDetails