SAT_SYNY3
ID SAT_SYNY3 Reviewed; 390 AA.
AC P74241;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 131.
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=slr1165;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA18335.1; -; Genomic_DNA.
DR PIR; S75876; S75876.
DR AlphaFoldDB; P74241; -.
DR SMR; P74241; -.
DR IntAct; P74241; 2.
DR STRING; 1148.1653421; -.
DR PaxDb; P74241; -.
DR EnsemblBacteria; BAA18335; BAA18335; BAA18335.
DR KEGG; syn:slr1165; -.
DR eggNOG; COG2046; Bacteria.
DR InParanoid; P74241; -.
DR OMA; LQHMIIR; -.
DR PhylomeDB; P74241; -.
DR BRENDA; 2.7.7.4; 382.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001425; 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..390
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105944"
SQ SEQUENCE 390 AA; 43696 MW; 8FDC66838CD65995 CRC64;
MTTSLAAIAP HGGQLINRLA PEAERQEFLA IADKLPRVQL DERATSDLVM IAIGGFSPLK
GFMEQDDYEL VVEEMKLSNG LPWSVPVTLS VTEEVAAPLE VGSWVRLDNS AGKFIGVLEL
TQKYHYNKAH EAKNVYRTDD QAHPGVKVIY DQGPVNLAGP IWLLEREPHP LFPKYQIDPA
ASRQLFAERG WKTIVGFQTR NPIHRAHEYI QKCALEVVDG LFLHPLVGAT KSDDIPADVR
MRCYEIMVDN YFPKERVILG INPSAMRYAG PREAIFHALI RKNYGCTHFI VGRDHAGVGD
YYGTYDAQEI FDEFAPEALG IVPMKFEHAF YCKKTLQMAT TKTSPSGPED RIHLSGTKVR
ALLRDGQLPP PEFSRPEVAQ ELIRAMQGES