ID W4QCU9_9BACI Unreviewed; 376 AA.
AC W4QCU9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00033770};
DE EC=2.4.2.14 {ECO:0000256|ARBA:ARBA00011941};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|ARBA:ARBA00033776};
GN ORFNames=JCM9152_849 {ECO:0000313|EMBL:GAE29488.1};
OS Halalkalibacter hemicellulosilyticusJCM 9152.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=1236971 {ECO:0000313|EMBL:GAE29488.1, ECO:0000313|Proteomes:UP000018895};
RN [1] {ECO:0000313|EMBL:GAE29488.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9152 {ECO:0000313|EMBL:GAE29488.1};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT hemicellulosilyticus JCM 9152T.";
RL Genome Announc. 2:e01258-13(2014).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005209}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138}.
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:GAE29488.1}.
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DR EMBL; BAUU01000005; GAE29488.1; -; Genomic_DNA.
DR AlphaFoldDB; W4QCU9; -.
DR STRING; 1236971.JCM9152_849; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000018895; Unassembled WGS sequence.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR NCBIfam; TIGR01134; purF; 1.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF13537; GATase_7; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:GAE29488.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000018895};
KW Transferase {ECO:0000313|EMBL:GAE29488.1}.
FT DOMAIN 1..136
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 376 AA; 40998 MW; 419F82A915DB3FE9 CRC64;
MQPLMFRSQT GSIAIAHNGN LVNATSMKHQ LEGQGSIFQS TSDTEVVAHL IKRSGFASLE
EQFRNALTML KGAYALAVMN EQQLMIALDP NGLRPLSLGR LGDAYVVASE TCAFDIIGAE
YVREVEPGEL IVIDEDGLRS QRFSGTSNRA ICSMEYIYFA RPDSNLDEIN VHTSRKNLGK
QLAMESPVEA DVVTGVPDSS ISAAIGYAEQ SGIPYELGMI KNRYVGRTFI QPSQELREQG
VKMKLSPVRG VVEGKRVVMI DDSIVRGTTS KRIVNMLRDA GATEVHVRIS SPPIKHPCFY
GIDTSTSGEL IAANHSLEEM REMMGADSLA FLSTDGLMEG IGRSDDSPNC GQCLACFTGS
YPTEIYPDTL HPYAKV
//
