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Protein

Sulfate adenylyltransferase

Gene

sat

Organism
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + sulfate = diphosphate + adenylyl sulfate.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. sulfate adenylyltransferase (ATP) activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  2. sulfate assimilation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciAVIN572477:GCJK-1135-MONOMER.
MetaCyc:MONOMER-16062.
UniPathwayiUPA00140; UER00204.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfate adenylyltransferase (EC:2.7.7.4)
Alternative name(s):
ATP-sulfurylase
Sulfate adenylate transferase
Short name:
SAT
Gene namesi
Name:sat
Ordered Locus Names:Alvin_1118
OrganismiAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
Taxonomic identifieri572477 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium
ProteomesiUP000001441: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Sulfate adenylyltransferasePRO_0000105939Add
BLAST

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Helixi18 – 2811Combined sources
Beta strandi33 – 353Combined sources
Helixi38 – 4811Combined sources
Turni49 – 546Combined sources
Helixi61 – 7010Combined sources
Beta strandi86 – 883Combined sources
Helixi91 – 933Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi111 – 1166Combined sources
Beta strandi119 – 1224Combined sources
Helixi125 – 13612Combined sources
Helixi144 – 1496Combined sources
Beta strandi154 – 16310Combined sources
Helixi167 – 1726Combined sources
Turni174 – 1763Combined sources
Helixi180 – 19011Combined sources
Beta strandi193 – 20210Combined sources
Helixi206 – 21914Combined sources
Beta strandi222 – 2309Combined sources
Helixi240 – 25415Combined sources
Beta strandi260 – 2667Combined sources
Helixi274 – 28714Combined sources
Beta strandi290 – 2945Combined sources
Turni296 – 2994Combined sources
Helixi309 – 3168Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi333 – 3364Combined sources
Turni337 – 3404Combined sources
Beta strandi341 – 3444Combined sources
Helixi345 – 3473Combined sources
Helixi353 – 3553Combined sources
Helixi361 – 3699Combined sources
Turni376 – 3783Combined sources
Helixi381 – 39313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DNXX-ray1.60A/B1-397[»]
ProteinModelPortaliO66036.
SMRiO66036. Positions 1-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfate adenylyltransferase family.Curated

Phylogenomic databases

HOGENOMiHOG000069044.
KOiK00958.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00066. Sulf_adenylyltr.
InterProiIPR025980. ATP-Sase_PUA-like_dom.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR020792. SO4_adenylyltransferase_subgr.
IPR024951. Sulfurylase_cat_dom.
IPR002650. Sulphate_adenylyltransferase.
[Graphical view]
PfamiPF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00339. sopT. 1 hit.

Sequencei

Sequence statusi: Complete.

O66036-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKPVGSDEL RPRFVYDPEQ HHRLSSEAES LPSVIVSSQA AGNAVMLGAG
60 70 80 90 100
YFSPLDGFMN LADALSSAQS MTLTDGRFFP VPLLCLLESA DAIAGATRIA
110 120 130 140 150
LRDPNVEGNP VLAVMDVTAV EQVSDAQMAL MTEQVYGTSD PKHPGVETFN
160 170 180 190 200
SQGRTAISGP IQVLNFSYFQ TDFPDTFRTA VEIRHEIQER GWQKIVAFQT
210 220 230 240 250
RNPMHRAHEE LCKMAMEAVE ADGVVIHMLL GQLKPGDIPA PVRDAAIRTM
260 270 280 290 300
AELYFPPNTV MVTGYGFDML YAGPREAVLH AYFRQNMGAT HFIIGRDHAG
310 320 330 340 350
VGDYYGPFDA QTIFDDAVPT DVLAIEIFRA DNTAYSKKLG RVVMMRDAPD
360 370 380 390
HTPDDFIQLS GTRVREMLGQ GEAPPPEFSR PEVAQILMDY YRSLPQS
Length:397
Mass (Da):43,762
Last modified:August 1, 1998 - v1
Checksum:iAC8967081284ECB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84759 Genomic DNA. Translation: AAC23622.1.
CP001896 Genomic DNA. Translation: ADC62057.1.
RefSeqiWP_012970332.1. NC_013851.1.
YP_003443089.1. NC_013851.1.

Genome annotation databases

EnsemblBacteriaiADC62057; ADC62057; Alvin_1118.
GeneIDi8786462.
KEGGialv:Alvin_1118.
PATRICi31921993. VBIAllVin64954_1113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84759 Genomic DNA. Translation: AAC23622.1.
CP001896 Genomic DNA. Translation: ADC62057.1.
RefSeqiWP_012970332.1. NC_013851.1.
YP_003443089.1. NC_013851.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DNXX-ray1.60A/B1-397[»]
ProteinModelPortaliO66036.
SMRiO66036. Positions 1-394.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADC62057; ADC62057; Alvin_1118.
GeneIDi8786462.
KEGGialv:Alvin_1118.
PATRICi31921993. VBIAllVin64954_1113.

Phylogenomic databases

HOGENOMiHOG000069044.
KOiK00958.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00204.
BioCyciAVIN572477:GCJK-1135-MONOMER.
MetaCyc:MONOMER-16062.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00066. Sulf_adenylyltr.
InterProiIPR025980. ATP-Sase_PUA-like_dom.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR020792. SO4_adenylyltransferase_subgr.
IPR024951. Sulfurylase_cat_dom.
IPR002650. Sulphate_adenylyltransferase.
[Graphical view]
PfamiPF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00339. sopT. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Towards the phylogeny of APS reductases and sirohaem sulfite reductases in sulfate-reducing and sulfur-oxidizing prokaryotes."
    Hipp W.M., Pott A.S., Thum-Schmitz N., Faath I., Dahl C., Trueper H.G.
    Microbiology 143:2891-2902(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome of Allochromatium vinosum DSM 180."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T.
    Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.

Entry informationi

Entry nameiSAT_ALLVD
AccessioniPrimary (citable) accession number: O66036
Secondary accession number(s): D3RS98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: February 4, 2015
This is version 85 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

3D-structure, Complete proteome, Reference proteome

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

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 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.