ID   CYSD_MYCBO              Reviewed;         309 AA.
AC   P65671; A0A1R3XXX9; Q10599; X2BHM7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   04-NOV-2026, entry version 110.
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};
GN   OrderedLocusNames=BQ2027_MB1316;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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=sulfate + ATP + H(+) = 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, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIT99919.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; LT708304; SIT99919.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P65671; -.
DR   SMR; P65671; -.
DR   KEGG; mbo:BQ2027_MB1316; -.
DR   PATRIC; fig|233413.5.peg.1442; -.
DR   OMA; AAQFHKP; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   FunFam; 3.40.50.620:FF:000002; Sulfate adenylyltransferase subunit 2; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00064; Sulf_adenylyltr_sub2; 1.
DR   InterPro; IPR002500; PAPS_reduct_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR   InterPro; IPR050128; Sulfate_adenylyltrnsfr_sub2.
DR   NCBIfam; TIGR02039; CysD; 1.
DR   NCBIfam; NF003587; cysD; 1.
DR   NCBIfam; NF009214; cysD; 1.
DR   PANTHER; PTHR43196; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR   PANTHER; PTHR43196:SF1; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF002936; CysDAde_trans; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..309
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100668"
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
//