PUR3_MYCTU
ID PUR3_MYCTU Reviewed; 215 AA.
AC P9WHM5; 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 40.
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=Rv0956;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-215 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=19394344; DOI=10.1016/j.jmb.2009.04.044;
RA Zhang Z., Caradoc-Davies T.T., Dickson J.M., Baker E.N., Squire C.J.;
RT "Structures of glycinamide ribonucleotide transformylase (PurN) from
RT Mycobacterium tuberculosis reveal a novel dimer with relevance to drug
RT discovery.";
RL J. Mol. Biol. 389:722-733(2009).
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19394344}.
CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000255|HAMAP-
CC Rule:MF_01930}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP43704.1; -; Genomic_DNA.
DR PIR; B70717; B70717.
DR RefSeq; NP_215471.1; NC_000962.3.
DR RefSeq; WP_003898661.1; NZ_NVQJ01000001.1.
DR PDB; 3DA8; X-ray; 1.30 A; A/B=2-215.
DR PDB; 3DCJ; X-ray; 2.20 A; A/B=2-215.
DR PDBsum; 3DA8; -.
DR PDBsum; 3DCJ; -.
DR AlphaFoldDB; P9WHM5; -.
DR SMR; P9WHM5; -.
DR STRING; 83332.Rv0956; -.
DR PaxDb; P9WHM5; -.
DR DNASU; 885407; -.
DR GeneID; 885407; -.
DR KEGG; mtu:Rv0956; -.
DR TubercuList; Rv0956; -.
DR eggNOG; COG0299; Bacteria.
DR OMA; TGITIHY; -.
DR PhylomeDB; P9WHM5; -.
DR BRENDA; 2.1.2.2; 3445.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
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 GO; GO:0046653; P:tetrahydrofolate metabolic process; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Purine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..215
FT /note="Phosphoribosylglycinamide formyltransferase"
FT /id="PRO_0000420698"
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 100..102
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT BINDING 116
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 150..154
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT SITE 154
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 11..21
FT /evidence="ECO:0007829|PDB:3DA8"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:3DA8"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3DA8"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3DA8"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3DA8"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:3DA8"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3DA8"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:3DA8"
FT HELIX 172..197
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3DA8"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3DA8"
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
