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Protein
Submitted name:

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase

Gene

nbaD

Organism
Pseudomonas fluorescens
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Iron; via tele nitrogenCombined sources
Metal bindingi9 – 91Zinc; via tele nitrogenCombined sources
Metal bindingi11 – 111Iron; via tele nitrogenCombined sources
Metal bindingi11 – 111Zinc; via tele nitrogenCombined sources
Metal bindingi177 – 1771Iron; via tele nitrogenCombined sources
Metal bindingi177 – 1771Zinc; via tele nitrogenCombined sources
Metal bindingi294 – 2941IronCombined sources
Metal bindingi294 – 2941ZincCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

IronCombined sources, Metal-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13360.
BRENDAi4.1.1.45. 5121.

Names & Taxonomyi

Protein namesi
Submitted name:
2-amino-3-carboxymuconate 6-semialdehyde decarboxylaseImported
Gene namesi
Name:nbaDImported
OrganismiPseudomonas fluorescensImported
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HBVX-ray1.65A/B1-334[»]
2HBXX-ray2.50A/B1-334[»]
4EPKX-ray2.60A/B1-334[»]
4ERAX-ray2.40A/B1-334[»]
4ERGX-ray2.79A/B1-334[»]
4ERIX-ray2.00A/B1-334[»]
4IFKX-ray2.01A/B3-333[»]
4IFOX-ray2.50A/B3-333[»]
4IFRX-ray2.39A/B4-333[»]
4IG2X-ray1.80A/B3-333[»]
ProteinModelPortaliQ83V25.
SMRiQ83V25. Positions 3-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ83V25.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 331326Amidohydro-relInterPro annotationAdd
BLAST

Family and domain databases

InterProiIPR032465. ACMSD.
IPR006680. Amidohydro-rel.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR21240:SF3. PTHR21240:SF3. 1 hit.
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.

Sequencei

Sequence statusi: Complete.

Q83V25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKPRIDMHS HFFPRISEQE AAKFDANHAP WLQVSAKGDT GSIMMGKNNF
60 70 80 90 100
RPVYQALWDP AFRIEEMDAQ GVDVQVTCAT PVMFGYTWEA NKAAQWAERM
110 120 130 140 150
NDFALEFAAH NPQRIKVLAQ VPLQDLDLAC KEASRAVAAG HLGIQIGNHL
160 170 180 190 200
GDKDLDDATL EAFLTHCANE DIPILVHPWD MMGGQRMKKW MLPWLVAMPA
210 220 230 240 250
ETQLAILSLI LSGAFERIPK SLKICFGHGG GSFAFLLGRV DNAWRHRDIV
260 270 280 290 300
REDCPRPPSE YVDRFFVDSA VFNPGALELL VSVMGEDRVM LGSDYPFPLG
310 320 330
EQKIGGLVLS SNLGESAKDK IISGNASKFF NINV
Length:334
Mass (Da):37,141
Last modified:June 1, 2003 - v1
Checksum:i231A6AF37CCD956C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088043 Genomic DNA. Translation: BAC65312.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088043 Genomic DNA. Translation: BAC65312.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HBVX-ray1.65A/B1-334[»]
2HBXX-ray2.50A/B1-334[»]
4EPKX-ray2.60A/B1-334[»]
4ERAX-ray2.40A/B1-334[»]
4ERGX-ray2.79A/B1-334[»]
4ERIX-ray2.00A/B1-334[»]
4IFKX-ray2.01A/B3-333[»]
4IFOX-ray2.50A/B3-333[»]
4IFRX-ray2.39A/B4-333[»]
4IG2X-ray1.80A/B3-333[»]
ProteinModelPortaliQ83V25.
SMRiQ83V25. Positions 3-334.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13360.
BRENDAi4.1.1.45. 5121.

Miscellaneous databases

EvolutionaryTraceiQ83V25.

Family and domain databases

InterProiIPR032465. ACMSD.
IPR006680. Amidohydro-rel.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR21240:SF3. PTHR21240:SF3. 1 hit.
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7."
    Muraki T., Taki M., Hasegawa Y., Iwaki H., Lau P.C.K.
    Appl. Environ. Microbiol. 69:1564-1572(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase: insight into the active site and catalytic mechanism of a novel decarboxylation reaction."
    Martynowski D., Eyobo Y., Li T., Yang K., Liu A., Zhang H.
    Biochemistry 45:10412-10421(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ZINC.
  3. "Evidence for a dual role of an active site histidine in alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase."
    Huo L., Fielding A.J., Chen Y., Li T., Iwaki H., Hosler J.P., Chen L., Hasegawa Y., Que L., Liu A.
    Biochemistry 51:5811-5821(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON AND ZINC.
  4. "The power of two: arginine 51 and arginine 239* from a neighboring subunit are essential for catalysis in alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase."
    Huo L., Davis I., Chen L., Liu A.
    J. Biol. Chem. 288:30862-30871(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-333 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiQ83V25_PSEFL
AccessioniPrimary (citable) accession number: Q83V25
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.