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P00436

- PCXA_PSEPU

UniProt

P00436 - PCXA_PSEPU

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Protein
Protocatechuate 3,4-dioxygenase alpha chain
Gene
pcaG
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.

Catalytic activityi

3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate.

Cofactori

Binds Fe3+ ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341Protocatechuate Reviewed prediction

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. protocatechuate 3,4-dioxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. beta-ketoadipate pathway Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Iron

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3186.
RETL1328306-WGS:GSTH-5904-MONOMER.
UniPathwayiUPA00157; UER00264.

Names & Taxonomyi

Protein namesi
Recommended name:
Protocatechuate 3,4-dioxygenase alpha chain (EC:1.13.11.3)
Alternative name(s):
3,4-PCD
Gene namesi
Name:pcaG
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 201200Protocatechuate 3,4-dioxygenase alpha chain
PRO_0000085095Add
BLAST

Interactioni

Subunit structurei

The enzyme is an oligomer of 12 copies of the alpha and beta chains.

Protein-protein interaction databases

IntActiP00436. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 225
Turni24 – 285
Beta strandi45 – 473
Beta strandi49 – 546
Beta strandi68 – 725
Beta strandi88 – 903
Beta strandi92 – 976
Turni100 – 1023
Beta strandi104 – 1107
Beta strandi127 – 1326
Beta strandi140 – 1467
Helixi147 – 1493
Helixi150 – 1545
Helixi159 – 1613
Beta strandi162 – 1643
Helixi165 – 1684
Helixi169 – 1713
Beta strandi172 – 1787
Beta strandi181 – 1855

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YKKX-ray2.06A/C/E/G/I/K2-201[»]
1YKLX-ray2.25A/C/E/G/I/K2-201[»]
1YKMX-ray2.22A/C/E/G/I/K2-201[»]
1YKNX-ray2.06A/C/E/G/I/K2-201[»]
1YKOX-ray2.54A/C/E/G/I/K2-201[»]
1YKPX-ray2.41A/C/E/G/I/K2-201[»]
2PCDX-ray2.15A/B/C/D/E/F2-201[»]
3LKTX-ray1.65A/B/C/D/E/F2-201[»]
3LMXX-ray2.20A/B/C2-201[»]
3LXVX-ray1.90A/B/C2-201[»]
3MFLX-ray1.78A/B/C2-201[»]
3MI1X-ray1.74A/B/C2-201[»]
3MI5X-ray1.78A/B/C/D/E/F2-201[»]
3MV4X-ray1.59A/B/C2-201[»]
3MV6X-ray1.86A/B/C2-201[»]
3PCAX-ray2.20A/B/C/D/E/F2-201[»]
3PCBX-ray2.19A/B/C/D/E/F2-201[»]
3PCCX-ray1.98A/B/C/D/E/F2-201[»]
3PCDX-ray2.10A/B/C/D/E/F2-201[»]
3PCEX-ray2.06A/B/C/D/E/F2-201[»]
3PCFX-ray2.15A/B/C/D/E/F2-201[»]
3PCGX-ray1.96A/B/C/D/E/F2-201[»]
3PCHX-ray2.05A/B/C/D/E/F2-201[»]
3PCIX-ray2.21A/B/C/D/E/F2-201[»]
3PCJX-ray2.13A/B/C/D/E/F2-201[»]
3PCKX-ray2.13A/B/C/D/E/F2-201[»]
3PCLX-ray2.15A/B/C/D/E/F2-201[»]
3PCMX-ray2.25A/B/C/D/E/F2-201[»]
3PCNX-ray2.40A/B/C/D/E/F2-201[»]
3T63X-ray1.54A/B/C2-201[»]
3T67X-ray1.67A/B/C2-201[»]
ProteinModelPortaliP00436.
SMRiP00436. Positions 2-201.

Miscellaneous databases

EvolutionaryTraceiP00436.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.130.10. 1 hit.
InterProiIPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
IPR012786. Protocat_dOase_a.
[Graphical view]
PfamiPF00775. Dioxygenase_C. 1 hit.
[Graphical view]
SUPFAMiSSF49482. SSF49482. 1 hit.
TIGRFAMsiTIGR02423. protocat_alph. 1 hit.
PROSITEiPS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00436-1 [UniParc]FASTAAdd to Basket

« Hide

MPIELLPETP SQTAGPYVHI GLALEAAGNP TRDQEIWNRL AKPDAPGEHI    50
LLLGQVYDGN GHLVRDSFLE VWQADANGEY QDAYNLENAF NSFGRTATTF 100
DAGEWTLHTV KPGVVNNAAG VPMAPHINIS LFARGINIHL HTRLYFDDEA 150
QANAKCPVLN LIEQPQRRET LIAKRCEVDG KTAYRFDIRI QGEGETVFFD 200
F 201
Length:201
Mass (Da):22,387
Last modified:January 23, 2007 - v3
Checksum:iBF95DB892076FBAF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601N → D AA sequence 1 Publication
Sequence conflicti77 – 771N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L14836 Genomic DNA. Translation: AAB41025.1.
PIRiB36930. DAPSAA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L14836 Genomic DNA. Translation: AAB41025.1 .
PIRi B36930. DAPSAA.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YKK X-ray 2.06 A/C/E/G/I/K 2-201 [» ]
1YKL X-ray 2.25 A/C/E/G/I/K 2-201 [» ]
1YKM X-ray 2.22 A/C/E/G/I/K 2-201 [» ]
1YKN X-ray 2.06 A/C/E/G/I/K 2-201 [» ]
1YKO X-ray 2.54 A/C/E/G/I/K 2-201 [» ]
1YKP X-ray 2.41 A/C/E/G/I/K 2-201 [» ]
2PCD X-ray 2.15 A/B/C/D/E/F 2-201 [» ]
3LKT X-ray 1.65 A/B/C/D/E/F 2-201 [» ]
3LMX X-ray 2.20 A/B/C 2-201 [» ]
3LXV X-ray 1.90 A/B/C 2-201 [» ]
3MFL X-ray 1.78 A/B/C 2-201 [» ]
3MI1 X-ray 1.74 A/B/C 2-201 [» ]
3MI5 X-ray 1.78 A/B/C/D/E/F 2-201 [» ]
3MV4 X-ray 1.59 A/B/C 2-201 [» ]
3MV6 X-ray 1.86 A/B/C 2-201 [» ]
3PCA X-ray 2.20 A/B/C/D/E/F 2-201 [» ]
3PCB X-ray 2.19 A/B/C/D/E/F 2-201 [» ]
3PCC X-ray 1.98 A/B/C/D/E/F 2-201 [» ]
3PCD X-ray 2.10 A/B/C/D/E/F 2-201 [» ]
3PCE X-ray 2.06 A/B/C/D/E/F 2-201 [» ]
3PCF X-ray 2.15 A/B/C/D/E/F 2-201 [» ]
3PCG X-ray 1.96 A/B/C/D/E/F 2-201 [» ]
3PCH X-ray 2.05 A/B/C/D/E/F 2-201 [» ]
3PCI X-ray 2.21 A/B/C/D/E/F 2-201 [» ]
3PCJ X-ray 2.13 A/B/C/D/E/F 2-201 [» ]
3PCK X-ray 2.13 A/B/C/D/E/F 2-201 [» ]
3PCL X-ray 2.15 A/B/C/D/E/F 2-201 [» ]
3PCM X-ray 2.25 A/B/C/D/E/F 2-201 [» ]
3PCN X-ray 2.40 A/B/C/D/E/F 2-201 [» ]
3T63 X-ray 1.54 A/B/C 2-201 [» ]
3T67 X-ray 1.67 A/B/C 2-201 [» ]
ProteinModelPortali P00436.
SMRi P00436. Positions 2-201.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00436. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00157 ; UER00264 .
BioCyci MetaCyc:MONOMER-3186.
RETL1328306-WGS:GSTH-5904-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00436.

Family and domain databases

Gene3Di 2.60.130.10. 1 hit.
InterProi IPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
IPR012786. Protocat_dOase_a.
[Graphical view ]
Pfami PF00775. Dioxygenase_C. 1 hit.
[Graphical view ]
SUPFAMi SSF49482. SSF49482. 1 hit.
TIGRFAMsi TIGR02423. protocat_alph. 1 hit.
PROSITEi PS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes."
    Frazee R.W., Livingston D.M., Laporte D.C., Lipscomb J.D.
    J. Bacteriol. 175:6194-6202(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
  2. "The primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase. II. Isolation and sequence of overlap peptides and complete sequence."
    Kohlmiller N.A., Howard J.B.
    J. Biol. Chem. 254:7309-7315(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-201.
    Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
  3. "Structure and assembly of protocatechuate 3,4-dioxygenase."
    Ohlendorf D.H., Lipscomb J.D., Weber P.C.
    Nature 336:403-405(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  4. "Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15-A resolution."
    Ohlendorf D.H., Orville A.M., Lipscomb J.D.
    J. Mol. Biol. 244:586-608(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
    Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
  5. "Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site."
    Orville A.M., Elango N., Lipscomb J.D., Ohlendorf D.H.
    Biochemistry 36:10039-10051(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
    Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
  6. "Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding."
    Orville A.M., Lipscomb J.D., Ohlendorf D.H.
    Biochemistry 36:10052-10066(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
    Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.
  7. "Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate."
    Elgren T.E., Orville A.M., Kelly K.A., Lipscomb J.D., Ohlendorf D.H., Que L. Jr.
    Biochemistry 36:11504-11513(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    Strain: ATCC 23975 / NCIMB 12602 / B-10 / Biotype A.

Entry informationi

Entry nameiPCXA_PSEPU
AccessioniPrimary (citable) accession number: P00436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Strain ATCC 23975 was originally classified as being from Pseudomonas aeruginosa.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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