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Database: UniProt
Entry: A0A089YSC7_9PSED
LinkDB: A0A089YSC7_9PSED
Original site: A0A089YSC7_9PSED 
ID   A0A089YSC7_9PSED        Unreviewed;       305 AA.
AC   A0A089YSC7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00064};
DE            EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00064};
DE   AltName: Full=ATP-sulfurylase small subunit {ECO:0000256|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00064};
DE            Short=SAT {ECO:0000256|HAMAP-Rule:MF_00064};
GN   Name=cysD {ECO:0000256|HAMAP-Rule:MF_00064};
GN   ORFNames=LT40_03925 {ECO:0000313|EMBL:AIS16600.1};
OS   Pseudomonas rhizosphaerae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS16600.1, ECO:0000313|Proteomes:UP000029499};
RN   [1] {ECO:0000313|EMBL:AIS16600.1, ECO:0000313|Proteomes:UP000029499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS16600.1};
RX   PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA   Kwak Y., Jung B.K., Shin J.H.;
RT   "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT   a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL   J. Biotechnol. 193:137-138(2015).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00064};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00064}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC       {ECO:0000256|HAMAP-Rule:MF_00064}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008885, ECO:0000256|HAMAP-Rule:MF_00064}.
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DR   EMBL; CP009533; AIS16600.1; -; Genomic_DNA.
DR   RefSeq; WP_043186772.1; NZ_CP009533.1.
DR   AlphaFoldDB; A0A089YSC7; -.
DR   STRING; 216142.LT40_03925; -.
DR   KEGG; prh:LT40_03925; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_6; -.
DR   OrthoDB; 9772604at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000029499; 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; HUPs; 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   NCBIfam; TIGR02039; 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 {ECO:0000256|HAMAP-Rule:MF_00064};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00064};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00064,
KW   ECO:0000313|EMBL:AIS16600.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:AIS16600.1}.
FT   DOMAIN          28..259
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
SQ   SEQUENCE   305 AA;  35248 MW;  FB86953AD11E7AF7 CRC64;
     MVDKLTHLKQ LEAESIHIIR EVAAEFDNPV MLYSIGKDSA VMLHLARKAF FPGKLPFPVM
     HVDTQWKFQE MYKFRDRMVE ELGLDLLVHV NPEGVAQGIN PFTHGSSKHT DIMKTQGLKQ
     ALDKYGFDAA FGGARRDEEK SRAKERVYSF RDSKHRWDPK NQRPELWNVY NGKVNKGESI
     RVFPLSNWTE LDIWQYIYLE GIPIVPLYFA AEREVIEKNG TLIMIDDERI LEHLSEEEKA
     SIVKKKVRFR TLGCYPLTGA VESEADSLTD IIQEMLLTRT SERQGRVIDH DGAGSMEDKK
     RQGYF
//
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