ID   CYSD1_CHRSD             Reviewed;         305 AA.
AC   Q1QWX0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 1 {ECO:0000255|HAMAP-Rule:MF_00064};
DE            EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00064};
DE   AltName: Full=ATP-sulfurylase small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase 1 {ECO:0000255|HAMAP-Rule:MF_00064};
DE            Short=SAT 1 {ECO:0000255|HAMAP-Rule:MF_00064};
GN   Name=cysD1 {ECO:0000255|HAMAP-Rule:MF_00064}; OrderedLocusNames=Csal_1686;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
CC   -!- FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the
CC       adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC       diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC       APS synthesis involves the formation of a high-energy phosphoric-
CC       sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC       to ATP hydrolysis by CysD. {ECO:0000255|HAMAP-Rule:MF_00064}.
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_00064};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00064}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC       {ECO:0000255|HAMAP-Rule:MF_00064}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00064}.
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DR   EMBL; CP000285; ABE59038.1; -; Genomic_DNA.
DR   RefSeq; WP_011506984.1; NC_007963.1.
DR   AlphaFoldDB; Q1QWX0; -.
DR   SMR; Q1QWX0; -.
DR   STRING; 290398.Csal_1686; -.
DR   EnsemblBacteria; ABE59038; ABE59038; Csal_1686.
DR   KEGG; csa:Csal_1686; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_6; -.
DR   OMA; LMIDTGH; -.
DR   OrthoDB; 499077at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000000239; 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   GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00064; Sulf_adenylyltr_sub2; 1.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF002936; CysDAde_trans; 1.
DR   TIGRFAMs; TIGR02039; CysD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..305
FT                   /note="Sulfate adenylyltransferase subunit 2 1"
FT                   /id="PRO_0000340192"
FT   REGION          283..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  35196 MW;  7090AE4282FACDF4 CRC64;
     MSGITPERQT HLKQLEAESI HIIREVAAEF ANPVMLYSIG KDSSVMLHLA RKAFYPGTPP
     FPLMHVNTTW KFKEMIEFRD RMAAEVGMEL IEHINEEGRA AGINPFDHGS AKYTDVMKTQ
     SLKQALDKYG FDAAFGGARR DEEASRAKER VYSFRDKHHR WDPKNQRPEL WNIYNGKVQK
     GESIRVFPLS NWTELDIWQY IYLESIPIVP LYYAAPRPVV ERDGMQIMVD DERLPLEDGE
     VPEEKWVRFR TLGCYPLTGA VESTAATLPE IIQEMLLTRT SERSGRAIDH DQAGSMERKK
     REGYF