ID A0A149Q3K9_9PROT Unreviewed; 264 AA.
AC A0A149Q3K9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=AD928_13915 {ECO:0000313|EMBL:KXU91803.1}, AD952_00685
GN {ECO:0000313|EMBL:KXV73152.1}, AD954_07845
GN {ECO:0000313|EMBL:KXV77566.1};
OS Acetobacter cerevisiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU91803.1, ECO:0000313|Proteomes:UP000075473};
RN [1] {ECO:0000313|Proteomes:UP000075312, ECO:0000313|Proteomes:UP000075462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1545 {ECO:0000313|EMBL:KXV77566.1,
RC ECO:0000313|Proteomes:UP000075462}, LMG 1608
RC {ECO:0000313|EMBL:KXV73152.1, ECO:0000313|Proteomes:UP000075312}, and
RC LMG 1625 {ECO:0000313|EMBL:KXU91803.1,
RC ECO:0000313|Proteomes:UP000075473};
RA Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT "Improved classification and identification of acetic acid bacteria using
RT matrix-assisted laser desorption/ionization time-of-flight mass
RT spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT respectively.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXU91803.1}.
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DR EMBL; LHZA01000157; KXU91803.1; -; Genomic_DNA.
DR EMBL; LHZY01000001; KXV73152.1; -; Genomic_DNA.
DR EMBL; LIAA01000032; KXV77566.1; -; Genomic_DNA.
DR RefSeq; WP_061491034.1; NZ_LIAA01000032.1.
DR AlphaFoldDB; A0A149Q3K9; -.
DR PATRIC; fig|178900.5.peg.535; -.
DR OrthoDB; 9772604at2; -.
DR Proteomes; UP000075312; Unassembled WGS sequence.
DR Proteomes; UP000075462; Unassembled WGS sequence.
DR Proteomes; UP000075473; Unassembled WGS sequence.
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:KXU91803.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075473};
KW Transferase {ECO:0000313|EMBL:KXU91803.1}.
FT DOMAIN 25..218
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 264 AA; 30418 MW; B50011C14AC382F4 CRC64;
MDHLDQLEAQ SVFILREAYR KLKPLAMLWS LGKDSNVMVW LAKKAFLGRV PFPVMHVDTG
KKFPEMYKFR DEYAKKWDLD LLLGTCPPVE EMDPSLPPAA RSAARKTAGL AAMIEKHKLQ
GVIAGIRRDE QGTRAKERVF SPRGASHKWD IRNQPPEFWD QYATPHEEGM HIRVHPLLSW
REIDIWRYIE REGIPLVDLY FAKNGKRYRS LGDQDITNPV ESNASTLAEV IAELETTRTS
ERSGRAMDHE SEDAFERLRV AGYL
//
