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P00437

- PCXB_PSEPU

UniProt

P00437 - PCXB_PSEPU

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Protein

Protocatechuate 3,4-dioxygenase beta chain

Gene

pcaH

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
Metal bindingi109 – 1091Iron; catalytic1 Publication
Metal bindingi148 – 1481Iron; catalytic1 Publication
Metal bindingi161 – 1611Iron; catalytic1 Publication
Metal bindingi163 – 1631Iron; catalytic1 Publication

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
  2. protocatechuate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3185.
RETL1328306-WGS:GSTH-5905-MONOMER.
UniPathwayiUPA00157; UER00264.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 239238Protocatechuate 3,4-dioxygenase beta chainPRO_0000085098Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP00437. 1 interaction.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Turni14 – 163Combined sources
Helixi26 – 283Combined sources
Turni29 – 313Combined sources
Helixi44 – 474Combined sources
Turni59 – 624Combined sources
Turni64 – 685Combined sources
Beta strandi70 – 723Combined sources
Beta strandi78 – 8710Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi136 – 1438Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi160 – 1667Combined sources
Turni171 – 1733Combined sources
Beta strandi175 – 1817Combined sources
Helixi187 – 1893Combined sources
Helixi193 – 1953Combined sources
Helixi199 – 2035Combined sources
Beta strandi206 – 2094Combined sources
Helixi211 – 2133Combined sources
Turni216 – 2183Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi231 – 2333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YKKX-ray2.06B/D/F/H/J/L2-239[»]
1YKLX-ray2.25B/D/F/H/J/L2-239[»]
1YKMX-ray2.22B/D/F/H/J/L2-239[»]
1YKNX-ray2.06B/D/F/H/J/L2-239[»]
1YKOX-ray2.54B/D/F/H/J/L2-239[»]
1YKPX-ray2.41B/D/F/H/J/L2-239[»]
2PCDX-ray2.15M/N/O/P/Q/R2-239[»]
3LKTX-ray1.65M/N/O/P/Q/R2-239[»]
3LMXX-ray2.20M/N/O2-239[»]
3LXVX-ray1.90M/N/O2-239[»]
3MFLX-ray1.78M/N/O2-239[»]
3MI1X-ray1.74M/N/O2-239[»]
3MI5X-ray1.78M/N/O/P/Q/R2-239[»]
3MV4X-ray1.59M/N/O2-239[»]
3MV6X-ray1.86M/N/O2-239[»]
3PCAX-ray2.20M/N/O/P/Q/R2-239[»]
3PCBX-ray2.19M/N/O/P/Q/R2-239[»]
3PCCX-ray1.98M/N/O/P/Q/R2-239[»]
3PCDX-ray2.10M/N/O/P/Q/R2-239[»]
3PCEX-ray2.06M/N/O/P/Q/R2-239[»]
3PCFX-ray2.15M/N/O/P/Q/R2-239[»]
3PCGX-ray1.96M/N/O/P/Q/R2-239[»]
3PCHX-ray2.05M/N/O/P/Q/R2-239[»]
3PCIX-ray2.21M/N/O/P/Q/R2-239[»]
3PCJX-ray2.13M/N/O/P/Q/R2-239[»]
3PCKX-ray2.13M/N/O/P/Q/R2-239[»]
3PCLX-ray2.15M/N/O/P/Q/R2-239[»]
3PCMX-ray2.25M/N/O/P/Q/R2-239[»]
3PCNX-ray2.40M/N/O/P/Q/R2-239[»]
3T63X-ray1.54M/N/O2-239[»]
3T67X-ray1.67M/N/O2-239[»]
ProteinModelPortaliP00437.
SMRiP00437. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00437.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.130.10. 1 hit.
InterProiIPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
IPR024756. PCDO_beta_N.
IPR012785. Protocat_dOase_b.
[Graphical view]
PfamiPF00775. Dioxygenase_C. 1 hit.
PF12391. PCDO_beta_N. 1 hit.
[Graphical view]
SUPFAMiSSF49482. SSF49482. 1 hit.
TIGRFAMsiTIGR02422. protocat_beta. 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.

P00437-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAQDNSRFV IRDRNWHPKA LTPDYKTSIA RSPRQALVSI PQSISETTGP
60 70 80 90 100
NFSHLGFGAH DHDLLLNFNN GGLPIGERII VAGRVVDQYG KPVPNTLVEM
110 120 130 140 150
WQANAGGRYR HKNDRYLAPL DPNFGGVGRC LTDSDGYYSF RTIKPGPYPW
160 170 180 190 200
RNGPNDWRPA HIHFGISGPS IATKLITQLY FEGDPLIPMC PIVKSIANPE
210 220 230
AVQQLIAKLD MNNANPMDCL AYRFDIVLRG QRKTHFENC
Length:239
Mass (Da):26,793
Last modified:January 23, 2007 - v3
Checksum:i8F8CC293B6E434CE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621H → D AA sequence (PubMed:115853)Curated
Sequence conflicti70 – 701N → D AA sequence (PubMed:115853)Curated
Sequence conflicti72 – 721Missing AA sequence (PubMed:115853)Curated
Sequence conflicti218 – 2181D → N AA sequence (PubMed:115853)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14836 Genomic DNA. Translation: AAB41024.1.
PIRiA36930. DAPSBA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14836 Genomic DNA. Translation: AAB41024.1 .
PIRi A36930. DAPSBA.

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 B/D/F/H/J/L 2-239 [» ]
1YKL X-ray 2.25 B/D/F/H/J/L 2-239 [» ]
1YKM X-ray 2.22 B/D/F/H/J/L 2-239 [» ]
1YKN X-ray 2.06 B/D/F/H/J/L 2-239 [» ]
1YKO X-ray 2.54 B/D/F/H/J/L 2-239 [» ]
1YKP X-ray 2.41 B/D/F/H/J/L 2-239 [» ]
2PCD X-ray 2.15 M/N/O/P/Q/R 2-239 [» ]
3LKT X-ray 1.65 M/N/O/P/Q/R 2-239 [» ]
3LMX X-ray 2.20 M/N/O 2-239 [» ]
3LXV X-ray 1.90 M/N/O 2-239 [» ]
3MFL X-ray 1.78 M/N/O 2-239 [» ]
3MI1 X-ray 1.74 M/N/O 2-239 [» ]
3MI5 X-ray 1.78 M/N/O/P/Q/R 2-239 [» ]
3MV4 X-ray 1.59 M/N/O 2-239 [» ]
3MV6 X-ray 1.86 M/N/O 2-239 [» ]
3PCA X-ray 2.20 M/N/O/P/Q/R 2-239 [» ]
3PCB X-ray 2.19 M/N/O/P/Q/R 2-239 [» ]
3PCC X-ray 1.98 M/N/O/P/Q/R 2-239 [» ]
3PCD X-ray 2.10 M/N/O/P/Q/R 2-239 [» ]
3PCE X-ray 2.06 M/N/O/P/Q/R 2-239 [» ]
3PCF X-ray 2.15 M/N/O/P/Q/R 2-239 [» ]
3PCG X-ray 1.96 M/N/O/P/Q/R 2-239 [» ]
3PCH X-ray 2.05 M/N/O/P/Q/R 2-239 [» ]
3PCI X-ray 2.21 M/N/O/P/Q/R 2-239 [» ]
3PCJ X-ray 2.13 M/N/O/P/Q/R 2-239 [» ]
3PCK X-ray 2.13 M/N/O/P/Q/R 2-239 [» ]
3PCL X-ray 2.15 M/N/O/P/Q/R 2-239 [» ]
3PCM X-ray 2.25 M/N/O/P/Q/R 2-239 [» ]
3PCN X-ray 2.40 M/N/O/P/Q/R 2-239 [» ]
3T63 X-ray 1.54 M/N/O 2-239 [» ]
3T67 X-ray 1.67 M/N/O 2-239 [» ]
ProteinModelPortali P00437.
SMRi P00437. Positions 2-239.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00437. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00157 ; UER00264 .
BioCyci MetaCyc:MONOMER-3185.
RETL1328306-WGS:GSTH-5905-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00437.

Family and domain databases

Gene3Di 2.60.130.10. 1 hit.
InterProi IPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
IPR024756. PCDO_beta_N.
IPR012785. Protocat_dOase_b.
[Graphical view ]
Pfami PF00775. Dioxygenase_C. 1 hit.
PF12391. PCDO_beta_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49482. SSF49482. 1 hit.
TIGRFAMsi TIGR02422. protocat_beta. 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 complete amino acid sequence of the beta-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa."
    Iwaki M., Kagamiyama H., Nozaki M.
    J. Biochem. 86:1159-1162(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-239.
  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 nameiPCXB_PSEPU
AccessioniPrimary (citable) accession number: P00437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 101 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