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SAT_CHLPB
ID   SAT_CHLPB               Reviewed;         404 AA.
AC   B3ELG8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Cphamn1_1839;
OS   Chlorobium phaeobacteroides (strain BS1).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=331678;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL   Submitted (JUN-2008) 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; CP001101; ACE04756.1; -; Genomic_DNA.
DR   RefSeq; WP_012475233.1; NC_010831.1.
DR   AlphaFoldDB; B3ELG8; -.
DR   SMR; B3ELG8; -.
DR   STRING; 331678.Cphamn1_1839; -.
DR   PRIDE; B3ELG8; -.
DR   KEGG; cpb:Cphamn1_1839; -.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_1_1_10; -.
DR   OMA; LQHMIIR; -.
DR   OrthoDB; 1574819at2; -.
DR   UniPathway; UPA00140; UER00204.
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; Transferase.
FT   CHAIN           1..404
FT                   /note="Sulfate adenylyltransferase"
FT                   /id="PRO_1000092255"
SQ   SEQUENCE   404 AA;  45121 MW;  6B781A072503FA59 CRC64;
     MPLVNPHGKD KVLKPLLLSG EELQNEMEKA KSLKEVRLSS RETGDLIMLG IGGFTPLEGF
     MGYDDWKGSV ENCMMADGTF WPIPITLSTS KELGDTLGIG EEVALVDDES GELMGSMVVE
     EKYEIDKAHE CREVFKTDNI EHPGVLQVMQ QGEVNLGGPV KVFSEGSFPS EFAGVYMTPA
     ETRALFEKNG WSTVAAFQTR NPMHRSHEYL VKIAIEICDG VLIHQLLGKL KPGDIPADVR
     KDSINALMEN YFVKGTCIQG GYPLDMRYAG PREALLHALF RQNFGCSHLI VGRDHAGVGD
     YYGPFDAHHI FDEIPRDALE TKPLKIDWTF YCYKCDGMAS MKTCPHGKDD RLSLSGTKLR
     KMLSEGEEVP DHFSRPEVLE ILKKYYAGLE EKVEVKMHTH AEGK
 
 
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