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
- Functionsferric iron binding / protocatechuate 3,4-dioxygenase activityProcessesbeta-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
- Dioxygenase_C (PF00775)
- 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
Resource Link UniProtKB ID P00436 UniProtKB Entry Name PCXA_PSEPU GenBank Protein ID 294344 GenBank Gene ID L14836 - General References
- 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]
- 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]
- Ohlendorf DH, Lipscomb JD, Weber PC: Structure and assembly of protocatechuate 3,4-dioxygenase. Nature. 1988 Nov 24;336(6197):403-5. [Article]
- 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]
- 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]
- 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]
- 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]