ID   CYSD_CAUSK              Reviewed;         305 AA.
AC   B0T3J3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 {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 {ECO:0000255|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00064};
DE            Short=SAT {ECO:0000255|HAMAP-Rule:MF_00064};
GN   Name=cysD {ECO:0000255|HAMAP-Rule:MF_00064}; OrderedLocusNames=Caul_1750;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABZ70879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000927; ABZ70879.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041538929.1; NC_010338.1.
DR   AlphaFoldDB; B0T3J3; -.
DR   SMR; B0T3J3; -.
DR   STRING; 366602.Caul_1750; -.
DR   EnsemblBacteria; ABZ70879; ABZ70879; Caul_1750.
DR   KEGG; cak:Caul_1750; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_5; -.
DR   OrthoDB; 499077at2; -.
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   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; Transferase.
FT   CHAIN           1..305
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000340191"
FT   REGION          283..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  35010 MW;  0D00ED59784C0C1A CRC64;
     MSVLSPARLT HLQRLEAESI HILREVAAEC ENPVMLYSIG KDSAVMLHLA AKAFYPSRPP
     FPLLHVDTTW KFRAMYELRD KVASDLGFDL LVHKNPEAEA RGINPFDHGS ALHTDLWKTE
     GLKQALAKYG FDAAFGGARR DEEKSRAKER VFSFRTTEQR WDPKDQRPEL WKLYNTRKHP
     GESLRVFPIS NWTELDVWQY IHLENIPIVP LYFAAERPVV ARDGSLIMVD DDRFRLRPGE
     VPQMKSVRFR TLGCYPLTGA VESTAATLPQ VIQEMLLTTT SERQGRVIDH DQSASMEKKK
     QEGYF