ID D5CSK9_SIDLE Unreviewed; 404 AA.
AC D5CSK9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00066};
DE AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_00066};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_00066};
GN Name=sat {ECO:0000256|HAMAP-Rule:MF_00066};
GN OrderedLocusNames=Slit_1712 {ECO:0000313|EMBL:ADE11945.1};
OS Sideroxydans lithotrophicus (strain ES-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Sideroxydans.
OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE11945.1, ECO:0000313|Proteomes:UP000001625};
RN [1] {ECO:0000313|EMBL:ADE11945.1, ECO:0000313|Proteomes:UP000001625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE11945.1,
RC ECO:0000313|Proteomes:UP000001625};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL Submitted (MAR-2010) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000262, ECO:0000256|HAMAP-
CC Rule:MF_00066};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|ARBA:ARBA00005048, ECO:0000256|HAMAP-
CC Rule:MF_00066}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00037980, ECO:0000256|HAMAP-Rule:MF_00066}.
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DR EMBL; CP001965; ADE11945.1; -; Genomic_DNA.
DR RefSeq; WP_013029843.1; NC_013959.1.
DR AlphaFoldDB; D5CSK9; -.
DR STRING; 580332.Slit_1712; -.
DR KEGG; slt:Slit_1712; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_4; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001625; 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; HUPs; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 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 NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR43509; -; 1.
DR PANTHER; PTHR43509:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00066};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00066};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00066}; Reference proteome {ECO:0000313|Proteomes:UP000001625};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00066}.
FT DOMAIN 5..163
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 174..384
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 404 AA; 44209 MW; FC5230DA6888C6F8 CRC64;
MALVNPHGGG DLKPLLLEGE ELIAEMKRAR SYPKVTVSSR EKGDLIMLGI GGFTPLDGFM
PHADWQGVCD GMTMTNGLFW PIPITLSTSK AAAEAIPTGT DIALVDPDDD SILATMKVTE
KYSIDKGHEC ATVFGTTDIE HPGVKMVMEQ GDVNLAGPVK VLSQGGFPQK YGTLFMTPKE
TRALFNELGW SKVAAFQTRN PMHRSHEYLA KVAIEVCDGV LIHSLLGNLK PGDIPAEVRT
QAIIALTKHY FVAKTIAQAG YPLDMRYAGP REALLHALFR QNYGCSHLIV GRDHAGVGSY
YGPFDAHHIF DKIPKGALET QALKIDWTFW CYKCGGMASA RTCPHGDADR LLLSGTKLRK
MLSEGSDVPA EFSRPEVLEI LREYYAGLQE HEKVEVKLTG HSAK
//
