ID   CYSD1_MARN8             Reviewed;         304 AA.
AC   A1U3Y0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase 1 {ECO:0000255|HAMAP-Rule:MF_00064};
DE            Short=SAT 1 {ECO:0000255|HAMAP-Rule:MF_00064};
GN   Name=cysD1 {ECO:0000255|HAMAP-Rule:MF_00064}; OrderedLocusNames=Maqu_2624;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(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 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; CP000514; ABM19699.1; -; Genomic_DNA.
DR   RefSeq; WP_011786070.1; NC_008740.1.
DR   AlphaFoldDB; A1U3Y0; -.
DR   SMR; A1U3Y0; -.
DR   STRING; 351348.Maqu_2624; -.
DR   EnsemblBacteria; ABM19699; ABM19699; Maqu_2624.
DR   KEGG; maq:Maqu_2624; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_6; -.
DR   OMA; LMIDTGH; -.
DR   OrthoDB; 499077at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000000998; 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; Transferase.
FT   CHAIN           1..304
FT                   /note="Sulfate adenylyltransferase subunit 2 1"
FT                   /id="PRO_0000340200"
SQ   SEQUENCE   304 AA;  34968 MW;  F100108C99B1014C CRC64;
     MTLTPPKKTH LKQLEAESIH IIREVAAEFD NPVMLYSIGK DSAVMLHLAM KAFAPGKPPF
     PLMHVDTTWK FREMITFRDQ MAEKLGMKLL VHTNQEGVEQ GIGPFTHGSA KHTDVMKTQA
     LKQALDKYGF DAAFGGARRD EEKSRAKERV YSFRDKFHRW DPKNQRPELW NLYNGKVNKG
     ESIRVFPLSN WTELDIWQYI YLENIDIVPL YYAAERPVVE RDGTLIMVDD DRMPLEPGEQ
     PMMKMVRFRT LGCYPLTGAV ESEAATLPDI IQEMLLTTTS ERQGRVIDHD GAASMEQKKR
     EGYF