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A8A1C2

- DCYD_ECOHS

UniProt

A8A1C2 - DCYD_ECOHS

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Protein
D-cysteine desulfhydrase
Gene
dcyD, EcHS_A2018
Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine By similarity.UniRule annotation

Catalytic activityi

D-cysteine + H2O = H2S + NH3 + pyruvate.UniRule annotation

Cofactori

Pyridoxal phosphate By similarity.UniRule annotation

GO - Molecular functioni

  1. D-cysteine desulfhydrase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-amino acid metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciECOL331112:GHHI-2010-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
D-cysteine desulfhydrase (EC:4.4.1.15)
Gene namesi
Name:dcyD
Ordered Locus Names:EcHS_A2018
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328D-cysteine desulfhydraseUniRule annotation
PRO_1000064261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi331112.EcHS_A2018.

Structurei

3D structure databases

ProteinModelPortaliA8A1C2.
SMRiA8A1C2. Positions 5-328.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2515.
HOGENOMiHOG000022459.
KOiK05396.
OMAiIMAQSFE.
OrthoDBiEOG6FBX0P.

Family and domain databases

HAMAPiMF_01045. D_Cys_desulfhydr.
InterProiIPR027278. ACCD_DCysDesulf.
IPR005966. D-Cys_desShydrase.
IPR023702. D_Cys_desulphydr_bac.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01275. ACC_deam_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

A8A1C2-1 [UniParc]FASTAAdd to Basket

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MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD DVTPMAMGGN    50
KLRKLEFLAA DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE 100
NPIGTTAENY LTNGNRLLLD LFNTQIEMCD ALTDPNAQLE ELATRVEAQG 150
FRPYVIPVGG SNALGALGYV ESALEIAQQC EGAVNISSVV VASGSAGTHA 200
GLAVGLEHLL PESELIGVTV SRSVADQLPK VVNLQQAIAK ELELTASAEI 250
LLWDDYFAPG YGVPNDEGME AVKLLARFEG ILLDPVYTGK AMAGLIDGIS 300
QKRFKDEGPI LFIHTGGAPA LFAYHPHV 328
Length:328
Mass (Da):35,169
Last modified:October 23, 2007 - v1
Checksum:i5079D3DF30B0521F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV06326.1.
RefSeqiYP_001458709.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV06326; ABV06326; EcHS_A2018.
GeneIDi5593828.
KEGGiecx:EcHS_A2018.
PATRICi18314014. VBIEscCol77814_1975.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV06326.1 .
RefSeqi YP_001458709.1. NC_009800.1.

3D structure databases

ProteinModelPortali A8A1C2.
SMRi A8A1C2. Positions 5-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331112.EcHS_A2018.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV06326 ; ABV06326 ; EcHS_A2018 .
GeneIDi 5593828.
KEGGi ecx:EcHS_A2018.
PATRICi 18314014. VBIEscCol77814_1975.

Phylogenomic databases

eggNOGi COG2515.
HOGENOMi HOG000022459.
KOi K05396.
OMAi IMAQSFE.
OrthoDBi EOG6FBX0P.

Enzyme and pathway databases

BioCyci ECOL331112:GHHI-2010-MONOMER.

Family and domain databases

HAMAPi MF_01045. D_Cys_desulfhydr.
InterProi IPR027278. ACCD_DCysDesulf.
IPR005966. D-Cys_desShydrase.
IPR023702. D_Cys_desulphydr_bac.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
PIRSFi PIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR01275. ACC_deam_rel. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiDCYD_ECOHS
AccessioniPrimary (citable) accession number: A8A1C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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