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Protein

Sulfate adenylyltransferase subunit 2

Gene

cysD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + sulfate = diphosphate + adenylyl sulfate.

Enzyme regulationi

Stimulated by an intrinsic GTPase (Probably CysN).

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sulfite from sulfate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Sulfate adenylyltransferase subunit 1 (cysN), Sulfate adenylyltransferase subunit 2 (cysD)
  2. Adenylyl-sulfate kinase (cysC)
  3. Phosphoadenosine phosphosulfate reductase (cysH)
This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sulfite from sulfate, the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • sulfate adenylyltransferase (ATP) activity Source: EcoCyc

GO - Biological processi

  • hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  • response to oxidative stress Source: EcoCyc
  • sulfate assimilation Source: UniProtKB-HAMAP
  • sulfate reduction Source: InterPro
  • sulfur compound metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CYSD-MONOMER.
ECOL316407:JW2722-MONOMER.
MetaCyc:CYSD-MONOMER.
SABIO-RKP21156.
UniPathwayiUPA00140; UER00204.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfate adenylyltransferase subunit 2 (EC:2.7.7.4)
Alternative name(s):
ATP-sulfurylase small subunit
Sulfate adenylate transferase
Short name:
SAT
Gene namesi
Name:cysD
Ordered Locus Names:b2752, JW2722
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10186. cysD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Sulfate adenylyltransferase subunit 2PRO_0000100664Add
BLAST

Proteomic databases

PaxDbiP21156.
PRIDEiP21156.

Interactioni

Subunit structurei

Heterodimer composed of CysD, the smaller subunit, and CysN.

Protein-protein interaction databases

BioGridi4263040. 15 interactions.
DIPiDIP-360N.
IntActiP21156. 5 interactions.
STRINGi511145.b2752.

Structurei

3D structure databases

ProteinModelPortaliP21156.
SMRiP21156. Positions 5-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAPS reductase family. CysD subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105C11. Bacteria.
COG0175. LUCA.
HOGENOMiHOG000263604.
InParanoidiP21156.
KOiK00957.
OMAiMHVDTTW.
OrthoDBiEOG6W45TZ.
PhylomeDBiP21156.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
HAMAPiMF_00064. Sulf_adenylyltr_sub2.
InterProiIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011784. SO4_adenylTrfase_ssu.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFiPIRSF002936. CysDAde_trans. 1 hit.
TIGRFAMsiTIGR02039. CysD. 1 hit.

Sequencei

Sequence statusi: Complete.

P21156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQIRLTHLR QLEAESIHII REVAAEFSNP VMLYSIGKDS SVMLHLARKA
60 70 80 90 100
FYPGTLPFPL LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI
110 120 130 140 150
NPFVHGSAKH TDIMKTEGLK QALNKYGFDA AFGGARRDEE KSRAKERIYS
160 170 180 190 200
FRDRFHRWDP KNQRPELWHN YNGQINKGES IRVFPLSNWT EQDIWQYIWL
210 220 230 240 250
ENIDIVPLYL AAERPVLERD GMLMMIDDNR IDLQPGEVIK KRMVRFRTLG
260 270 280 290 300
CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG

YF
Length:302
Mass (Da):35,188
Last modified:June 20, 2003 - v3
Checksum:iA48881C0E5E086A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti180 – 1801S → T in AAA23645 (PubMed:1316900).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74586 Genomic DNA. Translation: AAA23645.1.
U29579 Genomic DNA. Translation: AAA69262.1.
U00096 Genomic DNA. Translation: AAC75794.1.
AP009048 Genomic DNA. Translation: BAE76829.1.
M35098 Genomic DNA. Translation: AAA74892.1.
PIRiD65056.
RefSeqiNP_417232.1. NC_000913.3.
WP_000372108.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75794; AAC75794; b2752.
BAE76829; BAE76829; BAE76829.
GeneIDi947217.
KEGGiecj:JW2722.
eco:b2752.
PATRICi32120910. VBIEscCol129921_2847.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74586 Genomic DNA. Translation: AAA23645.1.
U29579 Genomic DNA. Translation: AAA69262.1.
U00096 Genomic DNA. Translation: AAC75794.1.
AP009048 Genomic DNA. Translation: BAE76829.1.
M35098 Genomic DNA. Translation: AAA74892.1.
PIRiD65056.
RefSeqiNP_417232.1. NC_000913.3.
WP_000372108.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP21156.
SMRiP21156. Positions 5-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263040. 15 interactions.
DIPiDIP-360N.
IntActiP21156. 5 interactions.
STRINGi511145.b2752.

Proteomic databases

PaxDbiP21156.
PRIDEiP21156.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75794; AAC75794; b2752.
BAE76829; BAE76829; BAE76829.
GeneIDi947217.
KEGGiecj:JW2722.
eco:b2752.
PATRICi32120910. VBIEscCol129921_2847.

Organism-specific databases

EchoBASEiEB0183.
EcoGeneiEG10186. cysD.

Phylogenomic databases

eggNOGiENOG4105C11. Bacteria.
COG0175. LUCA.
HOGENOMiHOG000263604.
InParanoidiP21156.
KOiK00957.
OMAiMHVDTTW.
OrthoDBiEOG6W45TZ.
PhylomeDBiP21156.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00204.
BioCyciEcoCyc:CYSD-MONOMER.
ECOL316407:JW2722-MONOMER.
MetaCyc:CYSD-MONOMER.
SABIO-RKP21156.

Miscellaneous databases

PROiP21156.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
HAMAPiMF_00064. Sulf_adenylyltr_sub2.
InterProiIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011784. SO4_adenylTrfase_ssu.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFiPIRSF002936. CysDAde_trans. 1 hit.
TIGRFAMsiTIGR02039. CysD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the sulfate activation locus from Escherichia coli K-12."
    Leyh T.S., Vogt T.F., Suo Y.
    J. Biol. Chem. 267:10405-10410(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Promoter elements and regulation of expression of the cysD gene of Escherichia coli K-12."
    Malo M.S., Loughlin R.E.
    Gene 87:127-131(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
    Strain: K12.
  5. "The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization."
    Leyh T.S., Taylor J.C., Markham G.D.
    J. Biol. Chem. 263:2409-2416(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiCYSD_ECOLI
AccessioniPrimary (citable) accession number: P21156
Secondary accession number(s): Q2MA77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: June 20, 2003
Last modified: January 20, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.