CYSD_VIBVU
ID CYSD_VIBVU Reviewed; 302 AA.
AC Q8DE72;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=VV1_0726;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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}.
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DR EMBL; AE016795; AAO09235.1; -; Genomic_DNA.
DR RefSeq; WP_011078801.1; NC_004459.3.
DR AlphaFoldDB; Q8DE72; -.
DR SMR; Q8DE72; -.
DR EnsemblBacteria; AAO09235; AAO09235; VV1_0726.
DR GeneID; 66963749; -.
DR KEGG; vvu:VV1_0726; -.
DR HOGENOM; CLU_043026_0_0_6; -.
DR OMA; MMILAED; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002275; Chromosome 1.
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..302
FT /note="Sulfate adenylyltransferase subunit 2"
FT /id="PRO_0000100679"
FT REGION 280..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 34972 MW; A036ECF9CEDE0669 CRC64;
MDQQRLTHLK QLEAESIHII REVAAEFDNP VMMYSIGKDS SVMLHLARKA FYPGKIPFPL
LHVDTDWKFR EMIEFRDRTA EKYGFELLVH KNPEGLAMGC SPFTHGSSKH TDIMKTQGLK
QALNKYGFDA AFGGARRDEE KSRAKERVYS FRDKNHTWDP KNQRPELWKT YNGQVNKGES
IRVFPLSNWT ELDIWQYIYL ENIEIVPLYL AAKRPVVERD GMLIMVDDDR MKLKEGEVIE
EKSVRFRTLG CYPLTGAIES EANTLTGIIE EMLVATSSER QGRAIDHDQS GSMELKKRQG
YF