SAT_SYNFM
ID SAT_SYNFM Reviewed; 410 AA.
AC A0LH38;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Sfum_1046;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK16740.1; -; Genomic_DNA.
DR RefSeq; WP_011697911.1; NC_008554.1.
DR AlphaFoldDB; A0LH38; -.
DR SMR; A0LH38; -.
DR STRING; 335543.Sfum_1046; -.
DR EnsemblBacteria; ABK16740; ABK16740; Sfum_1046.
DR KEGG; sfu:Sfum_1046; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_7; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001784; 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..410
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000340637"
SQ SEQUENCE 410 AA; 45491 MW; 37795DF74FF78D4B CRC64;
MSKLVPPHGK EKKLKPLLLE GAALAAEKEK AKTLKVVPMT SREASDLIML GIGAFTPLDG
FMGYADWKGV CDKYTMADGV FWPIPITLSA DKAVADSIGK NEEVALLDVE NNEILGTMKV
TEKYTIDKEH ECKSVFWTND AAGHPGVAKV MAQKEVNLAG PVKVISESFY PTQFKNVYQR
PAEARKLFDE KGWRRVAALQ LRNPMHRSHE FLAKIAVEVM DGLYIHQLVG KLKEGDIPAD
VRVKAIDVLV ENYFVKDTVI QGGYPAEMRY AGPREALLHA VFRQNYGCSH LIVGRDHAGV
GDYYGPFDAQ KIFDDIPEGA LLLQPLKIDW TFHCFKCGGM ASMRTCPHGK ADRLLLSGTM
VRKTLSEGGE LPKEFSRPEV VKVLQEYYAG LEEKVEIKLH GAATGDVKKK