GenomeNet

Database: UniProt
Entry: A0A1V9UUX1_9PSED
LinkDB: A0A1V9UUX1_9PSED
Original site: A0A1V9UUX1_9PSED 
ID   A0A1V9UUX1_9PSED        Unreviewed;       305 AA.
AC   A0A1V9UUX1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BWR59_09290 {ECO:0000313|EMBL:OQR33519.1};
OS   Pseudomonas sp. Bc-h.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1943632 {ECO:0000313|EMBL:OQR33519.1, ECO:0000313|Proteomes:UP000192462};
RN   [1] {ECO:0000313|EMBL:OQR33519.1, ECO:0000313|Proteomes:UP000192462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bc-h {ECO:0000313|EMBL:OQR33519.1,
RC   ECO:0000313|Proteomes:UP000192462};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQR33519.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MUIN01000005; OQR33519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9UUX1; -.
DR   STRING; 1943632.BWR59_09290; -.
DR   OrthoDB; 9772604at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000192462; Unassembled WGS sequence.
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:OQR33519.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:OQR33519.1}.
FT   DOMAIN          28..259
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
SQ   SEQUENCE   305 AA;  35390 MW;  10F18628FE96E5B2 CRC64;
     MVDKLTHLKQ LEAESIHIIR EVAAEFDNPV MLYSVGKDSA VMLHLARKAF FPGKLPFPVM
     HVDTRWKFQE MYRFRDQMVE DMGLDLIVHV NPDGVAQGIN PLTHGSAKHT DIMKTEGLKQ
     ALDKHGFDAA FGGARRDEEK SRAKERVYSF RDNKHRWDPK NQRPELWNVY NGNVNKGESI
     RVFPLSNWTE LDIWQYIYLE GIPIVPLYFA AEREVIEMNG TWIMIDDDRL RNHLSDEDKK
     RIVKKKVRFR TLGDYPLTGA VESEATSLTD IIQEMLLTRT SERQGRVIDH DGAGSMEEKK
     RQGYF
//
DBGET integrated database retrieval system