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O66036

- SAT_ALLVD

UniProt

O66036 - SAT_ALLVD

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
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    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

    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

    MIKPVGSDEL RPRFVYDPEQ HHRLSSEAES LPSVIVSSQA AGNAVMLGAG    50
    YFSPLDGFMN LADALSSAQS MTLTDGRFFP VPLLCLLESA DAIAGATRIA 100
    LRDPNVEGNP VLAVMDVTAV EQVSDAQMAL MTEQVYGTSD PKHPGVETFN 150
    SQGRTAISGP IQVLNFSYFQ TDFPDTFRTA VEIRHEIQER GWQKIVAFQT 200
    RNPMHRAHEE LCKMAMEAVE ADGVVIHMLL GQLKPGDIPA PVRDAAIRTM 250
    AELYFPPNTV MVTGYGFDML YAGPREAVLH AYFRQNMGAT HFIIGRDHAG 300
    VGDYYGPFDA QTIFDDAVPT DVLAIEIFRA DNTAYSKKLG RVVMMRDAPD 350
    HTPDDFIQLS GTRVREMLGQ GEAPPPEFSR PEVAQILMDY YRSLPQS 397
    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

    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