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O66036

- SAT_ALLVD

UniProt

O66036 - SAT_ALLVD

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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: 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-EC

GO - Biological processi

  1. hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  2. sulfate assimilation Source: InterPro
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 – 93
Helixi18 – 2811
Beta strandi33 – 353
Helixi38 – 4811
Turni49 – 546
Helixi61 – 7010
Beta strandi86 – 883
Helixi91 – 933
Beta strandi97 – 1026
Beta strandi111 – 1166
Beta strandi119 – 1224
Helixi125 – 13612
Helixi144 – 1496
Beta strandi154 – 16310
Helixi167 – 1726
Turni174 – 1763
Helixi180 – 19011
Beta strandi193 – 20210
Helixi206 – 21914
Beta strandi222 – 2309
Helixi240 – 25415
Beta strandi260 – 2667
Helixi274 – 28714
Beta strandi290 – 2945
Turni296 – 2994
Helixi309 – 3168
Beta strandi326 – 3294
Beta strandi333 – 3364
Turni337 – 3404
Beta strandi341 – 3444
Helixi345 – 3473
Helixi353 – 3553
Helixi361 – 3699
Turni376 – 3783
Helixi381 – 39313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U84759 Genomic DNA. Translation: AAC23622.1 .
CP001896 Genomic DNA. Translation: ADC62057.1 .
RefSeqi WP_012970332.1. NC_013851.1.
YP_003443089.1. NC_013851.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DNX X-ray 1.60 A/B 1-397 [» ]
ProteinModelPortali O66036.
SMRi O66036. Positions 1-394.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADC62057 ; ADC62057 ; Alvin_1118 .
GeneIDi 8786462.
KEGGi alv:Alvin_1118.
PATRICi 31921993. VBIAllVin64954_1113.

Phylogenomic databases

HOGENOMi HOG000069044.
KOi K00958.

Enzyme and pathway databases

UniPathwayi UPA00140 ; UER00204 .
BioCyci AVIN572477:GCJK-1135-MONOMER.
MetaCyc:MONOMER-16062.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00066. Sulf_adenylyltr.
InterProi IPR025980. 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 ]
Pfami PF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view ]
SUPFAMi SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR00339. sopT. 1 hit.
ProtoNeti Search...

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: October 1, 2014
This is version 82 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