ID B7L2N2_METC4 Unreviewed; 491 AA.
AC B7L2N2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE Short=ATase {ECO:0000256|HAMAP-Rule:MF_01931};
DE EC=2.4.2.14 {ECO:0000256|HAMAP-Rule:MF_01931};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
DE Short=GPATase {ECO:0000256|HAMAP-Rule:MF_01931};
GN Name=purF {ECO:0000256|HAMAP-Rule:MF_01931};
GN OrderedLocusNames=Mchl_4300 {ECO:0000313|EMBL:ACK85076.1};
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK85076.1, ECO:0000313|Proteomes:UP000002385};
RN [1] {ECO:0000313|Proteomes:UP000002385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACK85076.1, ECO:0000313|Proteomes:UP000002385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RX PubMed=22887658; DOI=10.1128/JB.01009-12;
RA Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M.,
RA Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E.,
RA Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N.,
RA Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M.,
RA Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.;
RT "Complete genome sequences of six strains of the genus Methylobacterium.";
RL J. Bacteriol. 194:4746-4748(2012).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000256|HAMAP-
CC Rule:MF_01931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRSR:PIRSR000485-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01931,
CC ECO:0000256|PIRSR:PIRSR000485-2};
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 ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138,
CC ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRNR:PIRNR000485}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01931}.
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DR EMBL; CP001298; ACK85076.1; -; Genomic_DNA.
DR RefSeq; WP_004446262.1; NC_011757.1.
DR AlphaFoldDB; B7L2N2; -.
DR MEROPS; C44.001; -.
DR GeneID; 72991648; -.
DR KEGG; mch:Mchl_4300; -.
DR HOGENOM; CLU_022389_3_1_5; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000002385; Chromosome.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd00715; GPATase_N; 1.
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 HAMAP; MF_01931; PurF; 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 InterPro; IPR035584; PurF_N.
DR NCBIfam; TIGR01134; purF; 1.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF13537; GATase_7; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 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 Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01931};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01931};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01931, ECO:0000256|PIRSR:PIRSR000485-
KW 2};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRSR:PIRSR000485-2};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01931};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931,
KW ECO:0000256|PIRNR:PIRNR000485}.
FT DOMAIN 24..243
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-1"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
FT BINDING 369
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01931,
FT ECO:0000256|PIRSR:PIRSR000485-2"
SQ SEQUENCE 491 AA; 53272 MW; AEC2D879245B5C32 CRC64;
MSVVSASADV RNLDIDGDTL REECGVFGIY GHDDASAITA LGLHALQHRG QEAAGIVSYD
DGVFHSERRQ GLVGDSFSDR ATIERLAGRS AIGHVRYSTT GGTILRNVQP LFAELAGGGL
AVAHNGNLTN ALSIRRDLVR DGAITQSTSD TEVILHLAAR SRKPRIVERF IDALQQIQGA
YAIVALTNKK LIGARDPLGI RPLVLGELDG RYILASESCA LDIIGARFIR DVENGEVVVI
SEEGVESIRF AEKQPMRPCI FEYIYFARPD SVVNGKSVYG VRKAIGQELA REAAPEADVV
IPVPDSGVPA ALGFAQEAGL PFEMGIIRNH YVGRTFIQPT QTVRELGVRM KHSANRAAVE
GKRIVLVDDS LVRGTTSVKI VRMMRDAGAR EVHFRIASPP ITYPDFYGID TPEREKLLAA
THDLEGMRQY IGADSLAFLS IPGLYRAMGE EARNADCPQY TDHCFTGDYP TGLTDLAIAG
PKRFAMLAEA D
//
