CYSD_ALIF1
ID CYSD_ALIF1 Reviewed; 302 AA.
AC Q5E831;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=VF_0320;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW84815.1; -; Genomic_DNA.
DR RefSeq; WP_005417374.1; NC_006840.2.
DR RefSeq; YP_203703.1; NC_006840.2.
DR AlphaFoldDB; Q5E831; -.
DR SMR; Q5E831; -.
DR STRING; 312309.VF_0320; -.
DR EnsemblBacteria; AAW84815; AAW84815; VF_0320.
DR GeneID; 64243325; -.
DR KEGG; vfi:VF_0320; -.
DR PATRIC; fig|312309.11.peg.313; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_043026_0_0_6; -.
DR OMA; LMIDTGH; -.
DR OrthoDB; 499077at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000000537; Chromosome I.
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..302
FT /note="Sulfate adenylyltransferase subunit 2"
FT /id="PRO_1000008998"
FT REGION 279..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; 35086 MW; 2EAE9C4DB29C1517 CRC64;
MDAKRLTHLQ QLEAESIHII REVAAEFDNP VMMYSIGKDS SVMLHLARKA FYPGKIPFPL
LHVDTDWKFK EMIEFRDKTA EKYGFDLLVH KNPEGLEMGI NPFVHGSSKH TDIMKTQGLK
QALNKYGFDA AFGGARRDEE KSRAKERVYS FRDKNHTWDP KNQRPELWNT YNGQVNKGES
IRVFPLSNWT ELDIWQYIYL ENIEIVPLYL SEKRPVVERD GMLIMVDDER LKLEEGEEIQ
HKDIRFRTLG CYPLTGAVES KANTLPEIIE EMLVATSSER QGRAIDHDSS GSMELKKRQG
YF
