ID   MMCV_STRLA              Reviewed;         319 AA.
AC   Q9X5U0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase small subunit;
DE   AltName: Full=Mitomycin biosynthesis protein V;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
GN   Name=mmcV;
OS   Streptomyces lavendulae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 2564;
RX   PubMed=10099135; DOI=10.1016/s1074-5521(99)80040-4;
RA   Mao Y.Q., Varoglu M., Sherman D.H.;
RT   "Molecular characterization and analysis of the biosynthetic gene cluster
RT   for the antitumor antibiotic mitomycin C from Streptomyces lavendulae NRRL
RT   2564.";
RL   Chem. Biol. 6:251-263(1999).
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.
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: Antibiotic biosynthesis; mitomycin C biosynthesis.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF127374; AAD32746.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X5U0; -.
DR   SMR; Q9X5U0; -.
DR   PRIDE; Q9X5U0; -.
DR   UniPathway; UPA00851; -.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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   Antibiotic biosynthesis; ATP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..319
FT                   /note="Sulfate adenylyltransferase subunit 2"
FT                   /id="PRO_0000100689"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  35856 MW;  66D929C9ECA3AF2B CRC64;
     MNPGRGGAYA AGRDGTRGTR RPHGLSHLDL LESESVHIFR EVAGEFERPV ILFSGGKDSI
     VMLHLALKSF APAPVPFALL HVDTGHNFPE VIAYRDRVVA ALGLRLEVAS VQDFIDNGTL
     RERPDGTRNP LQTVPLLDAI GRHRFDAVFG GGRRDEEKAR AKERVFSLRD EFGGWDPRRQ
     RPELWRLYNG RHAPGEHVRV FPLSNWTELD VWQYVAREEI ELPTIYYAHE REVFRRGGMW
     LAPGEWGGPR EGEAVEKRRV RYRTVGDMSC TGAVDSAAAT VADVVAEIAT SRLTERGATR
     ADDKLSEAAM EDRKREGYF