SAT_ALLVD
ID SAT_ALLVD Reviewed; 397 AA.
AC O66036; D3RS98;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=sat; OrderedLocusNames=Alvin_1118;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9308173; DOI=10.1099/00221287-143-9-2891;
RA Hipp W.M., Pott A.S., Thum-Schmitz N., Faath I., Dahl C., Trueper H.G.;
RT "Towards the phylogeny of APS reductases and sirohaem sulfite reductases in
RT sulfate-reducing and sulfur-oxidizing prokaryotes.";
RL Microbiology 143:2891-2902(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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 -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U84759; AAC23622.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC62057.1; -; Genomic_DNA.
DR RefSeq; WP_012970332.1; NC_013851.1.
DR PDB; 4DNX; X-ray; 1.60 A; A/B=1-397.
DR PDBsum; 4DNX; -.
DR AlphaFoldDB; O66036; -.
DR SMR; O66036; -.
DR STRING; 572477.Alvin_1118; -.
DR EnsemblBacteria; ADC62057; ADC62057; Alvin_1118.
DR KEGG; alv:Alvin_1118; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_6; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR BioCyc; MetaCyc:MON-16062; -.
DR BRENDA; 2.7.7.4; 257.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001441; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..397
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105939"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:4DNX"
FT TURN 49..54
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4DNX"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 240..254
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:4DNX"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:4DNX"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:4DNX"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:4DNX"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:4DNX"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:4DNX"
SQ SEQUENCE 397 AA; 43762 MW; AC8967081284ECB3 CRC64;
MIKPVGSDEL RPRFVYDPEQ HHRLSSEAES LPSVIVSSQA AGNAVMLGAG YFSPLDGFMN
LADALSSAQS MTLTDGRFFP VPLLCLLESA DAIAGATRIA LRDPNVEGNP VLAVMDVTAV
EQVSDAQMAL MTEQVYGTSD PKHPGVETFN SQGRTAISGP IQVLNFSYFQ TDFPDTFRTA
VEIRHEIQER GWQKIVAFQT RNPMHRAHEE LCKMAMEAVE ADGVVIHMLL GQLKPGDIPA
PVRDAAIRTM AELYFPPNTV MVTGYGFDML YAGPREAVLH AYFRQNMGAT HFIIGRDHAG
VGDYYGPFDA QTIFDDAVPT DVLAIEIFRA DNTAYSKKLG RVVMMRDAPD HTPDDFIQLS
GTRVREMLGQ GEAPPPEFSR PEVAQILMDY YRSLPQS
