ID   CYSD_MYCTU              Reviewed;         309 AA.
AC   P9WIK1; L0T670; P65670; Q10599;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 49.
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=Rv1285;
GN   ORFNames=MTCY373.04;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   SUBUNIT, AND INDUCTION.
RC   STRAIN=Mt103;
RX   PubMed=15184554; DOI=10.1099/mic.0.26894-0;
RA   Pinto R., Tang Q.X., Britton W.J., Leyh T.S., Triccas J.A.;
RT   "The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced
RT   operon that encodes a tri-functional sulfate-activating complex.";
RL   Microbiology 150:1681-1686(2004).
RN   [3]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(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 CysNC.
CC       {ECO:0000269|PubMed:15184554}.
CC   -!- INDUCTION: Induced by sulfur limitation and oxidative stress. Repressed
CC       by the presence of cysteine. {ECO:0000269|PubMed:15184554}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00064, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP44041.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL123456; CCP44041.1; ALT_INIT; Genomic_DNA.
DR   PIR; A70772; A70772.
DR   RefSeq; NP_215801.1; NC_000962.3.
DR   AlphaFoldDB; P9WIK1; -.
DR   SMR; P9WIK1; -.
DR   STRING; 83332.Rv1285; -.
DR   PaxDb; P9WIK1; -.
DR   DNASU; 886979; -.
DR   GeneID; 886979; -.
DR   KEGG; mtu:Rv1285; -.
DR   PATRIC; fig|83332.12.peg.1439; -.
DR   TubercuList; Rv1285; -.
DR   eggNOG; COG0175; Bacteria.
DR   OMA; LMIDTGH; -.
DR   Reactome; R-MTU-936635; Sulfate assimilation.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0009336; C:sulfate adenylyltransferase complex (ATP); IDA:MTBBASE.
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:0034599; P:cellular response to oxidative stress; IEP:MTBBASE.
DR   GO; GO:0010438; P:cellular response to sulfur starvation; IEP:MTBBASE.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IDA:MTBBASE.
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   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..309
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100667"
SQ   SEQUENCE   309 AA;  34889 MW;  75D965D35F1EC284 CRC64;
     MTSDVTVGPA PGQYQLSHLR LLEAEAIHVI REVAAEFERP VLLFSGGKDS IVMLHLALKA
     FRPGRLPFPV MHVDTGHNFD EVIATRDELV AAAGVRLVVA SVQDDIDAGR VVETIPSRNP
     IQTVTLLRAI RENQFDAAFG GARRDEEKAR AKERVFSFRD EFGQWDPKAQ RPELWNLYNG
     RHHKGEHIRV FPLSNWTEFD IWSYIGAEQV RLPSIYFAHR RKVFQRDGML LAVHRHMQPR
     ADEPVFEATV RFRTVGDVTC TGCVESSAST VAEVIAETAV ARLTERGATR ADDRISEAGM
     EDRKRQGYF