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Database: UniProt
Entry: Q5FSE7_GLUOX
LinkDB: Q5FSE7_GLUOX
Original site: Q5FSE7_GLUOX 
ID   Q5FSE7_GLUOX            Unreviewed;       285 AA.
AC   Q5FSE7;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 {ECO:0000256|ARBA:ARBA00022004};
DE            EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391};
DE   AltName: Full=ATP-sulfurylase small subunit {ECO:0000256|ARBA:ARBA00030256};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000256|ARBA:ARBA00031812};
GN   OrderedLocusNames=GOX0927 {ECO:0000313|EMBL:AAW60699.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60699.1, ECO:0000313|Proteomes:UP000006375};
RN   [1] {ECO:0000313|EMBL:AAW60699.1, ECO:0000313|Proteomes:UP000006375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H {ECO:0000313|EMBL:AAW60699.1,
RC   ECO:0000313|Proteomes:UP000006375};
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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         Evidence={ECO:0000256|ARBA:ARBA00000262};
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008885}.
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DR   EMBL; CP000009; AAW60699.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5FSE7; -.
DR   STRING; 290633.GOX0927; -.
DR   KEGG; gox:GOX0927; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_5; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011784; SO4_adenylTrfase_ssu.
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; 2.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000313|EMBL:AAW60699.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW   Transferase {ECO:0000313|EMBL:AAW60699.1}.
FT   DOMAIN          47..239
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
SQ   SEQUENCE   285 AA;  32920 MW;  F29DBC7670C6133A CRC64;
     MTQTRILSRD QSTTGLAQPR IMDDLDQLEA QSIFILREAY RKLKPLSLLW SLGKDSNVMV
     WLARKAFMGH VPFPVMHVDT EKKFPEMYAF RDEYTKKWNL DLLLGYCPPV EEIDPSLPPA
     ARSAARKTAG LAAMIDKHKF RGVIAGIRRD EQATRAKERV FSPRGAGHRW DVRNQPPEFW
     DQYATPYEDG MHIRVHPLLA WREIDIWRYI EREGIPLVDL YFAKDGKRYR SLGDQDITNP
     IESNASTVAE VIAELETSRT SERAGRAMDH ESEDVFERLR VAGYL
//
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