ID   PUR3_MYCTO              Reviewed;         215 AA.
AC   P9WHM4; F2GHX1; L0T6W9; P71554; Q7D921;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
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=MT0983;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45231.1; -; Genomic_DNA.
DR   PIR; B70717; B70717.
DR   RefSeq; WP_003898661.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHM4; -.
DR   SMR; P9WHM4; -.
DR   EnsemblBacteria; AAK45231; AAK45231; MT0983.
DR   KEGG; mtc:MT0983; -.
DR   PATRIC; fig|83331.31.peg.1055; -.
DR   HOGENOM; CLU_038395_1_0_11; -.
DR   UniPathway; UPA00074; UER00126.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
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   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00639; PurN; 1.
PE   3: Inferred from homology;
KW   Purine biosynthesis; Transferase.
FT   CHAIN           1..215
FT                   /note="Phosphoribosylglycinamide formyltransferase"
FT                   /id="PRO_0000428159"
FT   ACT_SITE        118
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT   BINDING         74
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT   BINDING         99..102
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT   BINDING         116
FT                   /ligand="(6S)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57454"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT   SITE            154
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
SQ   SEQUENCE   215 AA;  22416 MW;  55556C033097EAA1 CRC64;
     MQEPLRVPPS APARLVVLAS GTGSLLRSLL DAAVGDYPAR VVAVGVDREC RAAEIAAEAS
     VPVFTVRLAD HPSRDAWDVA ITAATAAHEP DLVVSAGFMR ILGPQFLSRF YGRTLNTHPA
     LLPAFPGTHG VADALAYGVK VTGATVHLVD AGTDTGPILA QQPVPVLDGD DEETLHERIK
     VTERRLLVAA VAALATHGVT VVGRTATMGR KVTIG