SAT_OCEIH
ID SAT_OCEIH Reviewed; 395 AA.
AC Q8EQN5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00066};
DE AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_00066};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_00066};
GN Name=sat {ECO:0000255|HAMAP-Rule:MF_00066}; OrderedLocusNames=OB1659;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00066};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00066}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00066}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000028; BAC13615.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8EQN5; -.
DR SMR; Q8EQN5; -.
DR STRING; 221109.22777342; -.
DR PRIDE; Q8EQN5; -.
DR EnsemblBacteria; BAC13615; BAC13615; BAC13615.
DR KEGG; oih:OB1659; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_9; -.
DR OMA; LQHMIIR; -.
DR PhylomeDB; Q8EQN5; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000000822; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00066; Sulf_adenylyltr; 1.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020792; SO4_adenylyltransferase_pro.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_1000009042"
SQ SEQUENCE 395 AA; 44784 MW; 89846301BDF070F8 CRC64;
MSSVEMKEQE NILPHGGELI DRELTGDRKE SYLHKSKSLL ALKLDAWSLS DLELIANGGF
SPLTGFMGEE DYQSVIENVC LKDGTVWSIP ITLAVNKEQA DSYDIGTSIA LFGEDDILYG
VLELEEKYTY EKEKEASLVY GTTDAAHPGV KKLYEKGDVY LAGPIFMLNR PSHDNFEKFY
YDPKETRKMF AELGWKTIVG FQTRNPVHRA HEYIQKSALE SVDGLLLNPL VGETKSDDIS
AEIRMESYQV ILKNYYPENR ARLVIYPAAM RYAGPKEAIL HAIVRKNYGC THFIVGRDHA
GVGDYYGTYE AQDLISQYEE KLGIQIFKFE HAFFCTKCEN MGTEKTCPHG KEFHVHLSGT
KVREKLRNGE QLPKEFSRPE VASVLMKGLS KNNTN