SAT_IGNH4
ID SAT_IGNH4 Reviewed; 382 AA.
AC A8AB48;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=Igni_0970;
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
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}.
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DR EMBL; CP000816; ABU82150.1; -; Genomic_DNA.
DR RefSeq; WP_012123114.1; NC_009776.1.
DR AlphaFoldDB; A8AB48; -.
DR SMR; A8AB48; -.
DR STRING; 453591.Igni_0970; -.
DR EnsemblBacteria; ABU82150; ABU82150; Igni_0970.
DR GeneID; 5561764; -.
DR KEGG; iho:Igni_0970; -.
DR eggNOG; arCOG04191; Archaea.
DR HOGENOM; CLU_022950_1_1_2; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 15586at2157; -.
DR PhylomeDB; A8AB48; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000000262; 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..382
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_1000009041"
SQ SEQUENCE 382 AA; 44062 MW; FD2378B183F987F5 CRC64;
MVSKPHGGKL VERVAKGKTR ERLVEEAKEM VNVQVDEGLA ADVANVAHGV YSPLEGFMVR
EDYLSVLEFM RLSNDLPWTI PIILDVDENV KKSVREGDEV AIFFKGKPIA ILYVEEIFPW
DKNYHTLKVF KTDDLNHPGV RKVFNKKDYL LGGPLIQISD VPEPFEKYRL WPKETRVLFE
QKGWKRVAAF QTRNVPHLGH EYVQKAALTF TDGLFVNPLV GWKKPGDFRD EVIIKAYEAL
IEHYYPKDSV AFSVLRMEMR YAGPREAVHH AIVRKNFGAT HFIVGRDHAG VGNYYGPYEA
WDIFKNFPDL GITPLFVREA FYCKKCGGMV NEKICPHPEE YRIRISGTKL RKMIMEGKRP
PEYMMRPEVA EVVLSFEDPF VH