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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

Fe3+Note: Binds Fe(3+) ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341ProtocatechuateSequence Analysis

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 chainPRO_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

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 225Combined sources
Turni24 – 285Combined sources
Beta strandi45 – 473Combined sources
Beta strandi49 – 546Combined sources
Beta strandi68 – 725Combined sources
Beta strandi88 – 903Combined sources
Beta strandi92 – 976Combined sources
Turni100 – 1023Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi140 – 1467Combined sources
Helixi147 – 1493Combined sources
Helixi150 – 1545Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1643Combined sources
Helixi165 – 1684Combined sources
Helixi169 – 1713Combined sources
Beta strandi172 – 1787Combined sources
Beta strandi181 – 1855Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MPIELLPETP SQTAGPYVHI GLALEAAGNP TRDQEIWNRL AKPDAPGEHI
60 70 80 90 100
LLLGQVYDGN GHLVRDSFLE VWQADANGEY QDAYNLENAF NSFGRTATTF
110 120 130 140 150
DAGEWTLHTV KPGVVNNAAG VPMAPHINIS LFARGINIHL HTRLYFDDEA
160 170 180 190 200
QANAKCPVLN LIEQPQRRET LIAKRCEVDG KTAYRFDIRI QGEGETVFFD

F
Length:201
Mass (Da):22,387
Last modified:January 23, 2007 - v3
Checksum:iBF95DB892076FBAF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601N → D AA sequence (PubMed:465136)Curated
Sequence conflicti77 – 771N → D AA sequence (PubMed:465136)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14836 Genomic DNA. Translation: AAB41025.1.
PIRiB36930. DAPSAA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14836 Genomic DNA. Translation: AAB41025.1 .
PIRi B36930. DAPSAA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 100 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.Curated

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