CYSD_RHIME
ID CYSD_RHIME Reviewed; 317 AA.
AC P56892;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Sulfate adenylyltransferase subunit 2;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase small subunit;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=cysD; OrderedLocusNames=R00943; ORFNames=SMc00091;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=10464198; DOI=10.1128/jb.181.17.5280-5287.1999;
RA Abola A.P., Willits M.G., Wang R.C., Long S.R.;
RT "Reduction of adenosine-5'-phosphosulfate instead of 3'-phosphoadenosine-
RT 5'-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other
RT members of the family Rhizobiaceae.";
RL J. Bacteriol. 181:5280-5287(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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:0000250}.
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;
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC {ECO:0000305}.
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DR EMBL; AF158023; AAD55760.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45515.1; -; Genomic_DNA.
DR RefSeq; NP_385049.1; NC_003047.1.
DR RefSeq; WP_003536273.1; NC_003047.1.
DR AlphaFoldDB; P56892; -.
DR SMR; P56892; -.
DR STRING; 266834.SMc00091; -.
DR EnsemblBacteria; CAC45515; CAC45515; SMc00091.
DR GeneID; 61602409; -.
DR KEGG; sme:SMc00091; -.
DR PATRIC; fig|266834.11.peg.2341; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_043026_0_0_5; -.
DR OMA; MMILAED; -.
DR BioCyc; MetaCyc:MON-16112; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001976; 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..317
FT /note="Sulfate adenylyltransferase subunit 2"
FT /id="PRO_0000100672"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 260
FT /note="R -> A (in Ref. 1; AAD55760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 36429 MW; 093F2724D22841CB CRC64;
MPHTLPETEL HNPQSTKPPL DPHLKALENE AIHIFREVAA EFERPVMLYS IGKDSSVLLH
LARKAFYPGR IPFPLLHVDT GWKFREMIAF RDEMVAKYDL DLVAHTNPRG AAENVTPFTH
GSALYTDIMK TEALRQALDA GQYDAAFGGA RRDEEASRAK ERIYSFRTPD HRWDPRNQRP
ELWNVYNGMI RKGESVRAFP LSNWTEVDIW RYIQAEDIPI VPLYFAKKRP VVERDGMLIL
AEDPRLELLP GEVKREEVIR FRTLGCFPLT GAIRSEADTL DDIIAELETA TVSERQGRAI
DRDQAGSMEK KKREGYF
