PUR3_HAEIN
ID PUR3_HAEIN Reviewed; 212 AA.
AC P43846;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01930};
DE EC=2.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01930};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000255|HAMAP-Rule:MF_01930};
DE AltName: Full=GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01930};
DE Short=GART {ECO:0000255|HAMAP-Rule:MF_01930};
GN Name=purN {ECO:0000255|HAMAP-Rule:MF_01930}; OrderedLocusNames=HI_1428;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 10-
CC formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR),
CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and
CC tetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286;
CC EC=2.1.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01930};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC ribosyl)glycinamide (10-formyl THF route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01930}.
CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000255|HAMAP-
CC Rule:MF_01930}.
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DR EMBL; L42023; AAC23075.1; -; Genomic_DNA.
DR PIR; F64122; F64122.
DR RefSeq; NP_439577.1; NC_000907.1.
DR RefSeq; WP_005693938.1; NC_000907.1.
DR AlphaFoldDB; P43846; -.
DR SMR; P43846; -.
DR STRING; 71421.HI_1428; -.
DR EnsemblBacteria; AAC23075; AAC23075; HI_1428.
DR KEGG; hin:HI_1428; -.
DR PATRIC; fig|71421.8.peg.1485; -.
DR eggNOG; COG0299; Bacteria.
DR HOGENOM; CLU_038395_1_1_6; -.
DR OMA; TGITIHY; -.
DR PhylomeDB; P43846; -.
DR BioCyc; HINF71421:G1GJ1-1451-MON; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR CDD; cd08645; FMT_core_GART; 1.
DR HAMAP; MF_01930; PurN; 1.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004607; GART.
DR InterPro; IPR001555; GART_AS.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00639; PurN; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Purine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..212
FT /note="Phosphoribosylglycinamide formyltransferase"
FT /id="PRO_0000074944"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 12..14
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 90..93
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 107
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT SITE 145
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
SQ SEQUENCE 212 AA; 23463 MW; D1AE249CDDB879C4 CRC64;
MKKIAVLISG QGTNLQTIID ACHSGDIPAK IACVISNKAD AYGLVRAKQA QIPQAVFLRK
NFSNNLEMDD AIGDYLQSLA VDLIVLAGYM KILTPKFTQR FAGKILNIHP SLLPKYAGLN
TYQRAIEAGD NEHGTTVHFV NEEVDGGAIV LQAKVPIFPE DSIEEVEART REQEYQIYPL
VIKWFTEGRL RLKDNLAYLD GKALPKSGYA NE
