ID Q2GLA4_ANAPZ Unreviewed; 211 AA.
AC Q2GLA4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01930};
DE EC=2.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01930};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|HAMAP-Rule:MF_01930};
DE AltName: Full=GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01930};
DE Short=GART {ECO:0000256|HAMAP-Rule:MF_01930};
GN Name=purN {ECO:0000256|HAMAP-Rule:MF_01930,
GN ECO:0000313|EMBL:ABD44447.1};
GN OrderedLocusNames=APH_0230 {ECO:0000313|EMBL:ABD44447.1};
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042 {ECO:0000313|EMBL:ABD44447.1, ECO:0000313|Proteomes:UP000001943};
RN [1] {ECO:0000313|EMBL:ABD44447.1, ECO:0000313|Proteomes:UP000001943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ {ECO:0000313|EMBL:ABD44447.1,
RC ECO:0000313|Proteomes:UP000001943};
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
RN [2] {ECO:0007829|PDB:3KCQ}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RG Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RA Staker B.L., Edwards T., Dieterich M.;
RT "Crystal structure of phosphoribosylglycinamide formyltransferase from
RT anaplasma phagocytophilum.";
RL Submitted (OCT-2009) to the PDB data bank.
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:0000256|HAMAP-Rule:MF_01930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-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:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366;
CC EC=2.1.2.2; Evidence={ECO:0000256|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:0000256|ARBA:ARBA00005054, ECO:0000256|HAMAP-Rule:MF_01930}.
CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|HAMAP-
CC Rule:MF_01930}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01930}.
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DR EMBL; CP000235; ABD44447.1; -; Genomic_DNA.
DR RefSeq; WP_011450370.1; NC_007797.1.
DR PDB; 3KCQ; X-ray; 2.20 A; A/B/C/D=1-211.
DR PDBsum; 3KCQ; -.
DR AlphaFoldDB; Q2GLA4; -.
DR SMR; Q2GLA4; -.
DR STRING; 212042.APH_0230; -.
DR PaxDb; 212042-APH_0230; -.
DR EnsemblBacteria; ABD44447; ABD44447; APH_0230.
DR GeneID; 56368385; -.
DR KEGG; aph:APH_0230; -.
DR PATRIC; fig|212042.8.peg.244; -.
DR eggNOG; COG0299; Bacteria.
DR HOGENOM; CLU_038395_1_1_5; -.
DR UniPathway; UPA00074; UER00126.
DR EvolutionaryTrace; Q2GLA4; -.
DR Proteomes; UP000001943; 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 Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 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 NCBIfam; TIGR00639; PurN; 1.
DR PANTHER; PTHR43369; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR43369:SF2; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3KCQ};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01930};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01930}.
FT DOMAIN 6..178
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT ACT_SITE 107
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 15..17
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 62
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 105
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT SITE 143
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ SEQUENCE 211 AA; 23192 MW; 4B1313933DB8BF3C CRC64;
MKKELRVGVL ISGRGSNLEA LAKAFSTEES SVVISCVISN NAEARGLLIA QSYGIPTFVV
KRKPLDIEHI STVLREHDVD LVCLAGFMSI LPEKFVTDWH HKIINIHPSL LPSFKGLNAQ
EQAYKAGVKI AGCTLHYVYQ ELDAGPIIMQ AAVPVLREDT AESLASRILA AEHVCYPKGV
KLIAQDKIKL CDDGTVQCTG EDELFLFQEN F
//
