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B1LQT7

- DCYD_ECOSM

UniProt

B1LQT7 - DCYD_ECOSM

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Protein

D-cysteine desulfhydrase

Gene

dcyD

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
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.UniRule annotation

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.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

BioCyciECOL439855:GHHB-1261-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
D-cysteine desulfhydraseUniRule annotation (EC:4.4.1.15UniRule annotation)
Gene namesi
Name:dcyDUniRule annotation
Ordered Locus Names:EcSMS35_1263
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328D-cysteine desulfhydrasePRO_1000136162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiB1LQT7.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi439855.EcSMS35_1263.

Structurei

3D structure databases

ProteinModelPortaliB1LQT7.
SMRiB1LQT7. Positions 7-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ACC deaminase/D-cysteine desulfhydrase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2515.
HOGENOMiHOG000022459.
KOiK05396.
OMAiPYLVPIG.
OrthoDBiEOG6FBX0P.

Family and domain databases

HAMAPiMF_01045. D_Cys_desulfhydr.
InterProiIPR027278. ACCD_DCysDesulf.
IPR005966. D-Cys_desShydrase.
IPR023702. D_Cys_desulphydr_bac.
IPR001926. TrpB-like_PLP-dep.
[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.

B1LQT7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD DVTPMAMGGN
60 70 80 90 100
KLRKLEFLAA DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE
110 120 130 140 150
NPIGTTAENY LTNGNRLLLD LFNTQIEMCD ALTDPNAQLE ELATRVEAQG
160 170 180 190 200
FRPYVIPVGG SNALGALGYV ESALEIAQQC EGAVNISSVV VASGSAGTHA
210 220 230 240 250
GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK ELELTASAEI
260 270 280 290 300
LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS
310 320
QKRFKDEGPI LFIHTGGAPA LFAYHPHV
Length:328
Mass (Da):35,153
Last modified:April 29, 2008 - v1
Checksum:i4179DE645C0B32D8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB19636.1.
RefSeqiYP_001743324.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB19636; ACB19636; EcSMS35_1263.
GeneIDi6144001.
KEGGiecm:EcSMS35_1263.
PATRICi18431393. VBIEscCol6161_1424.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB19636.1 .
RefSeqi YP_001743324.1. NC_010498.1.

3D structure databases

ProteinModelPortali B1LQT7.
SMRi B1LQT7. Positions 7-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439855.EcSMS35_1263.

Proteomic databases

PRIDEi B1LQT7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB19636 ; ACB19636 ; EcSMS35_1263 .
GeneIDi 6144001.
KEGGi ecm:EcSMS35_1263.
PATRICi 18431393. VBIEscCol6161_1424.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ECOL439855:GHHB-1261-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. TrpB-like_PLP-dep.
[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. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
    Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
    J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SMS-3-5 / SECEC.

Entry informationi

Entry nameiDCYD_ECOSM
AccessioniPrimary (citable) accession number: B1LQT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: October 29, 2014
This is version 43 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