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Database: UniProt/TrEMBL
Entry: K9P4Z9_CYAGP
LinkDB: K9P4Z9_CYAGP
Original site: K9P4Z9_CYAGP 
ID   K9P4Z9_CYAGP            Unreviewed;       219 AA.
AC   K9P4Z9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   OrderedLocusNames=Cyagr_0590 {ECO:0000313|EMBL:AFY27781.1};
OS   Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Cyanobium.
OX   NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY27781.1, ECO:0000313|Proteomes:UP000010388};
RN   [1] {ECO:0000313|Proteomes:UP000010388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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DR   EMBL; CP003495; AFY27781.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9P4Z9; -.
DR   STRING; 292564.Cyagr_0590; -.
DR   KEGG; cgc:Cyagr_0590; -.
DR   PATRIC; fig|292564.3.peg.546; -.
DR   eggNOG; COG0299; Bacteria.
DR   HOGENOM; CLU_038395_1_0_3; -.
DR   OrthoDB; 9806170at2; -.
DR   UniPathway; UPA00074; UER00126.
DR   Proteomes; UP000010388; 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   3: Inferred from homology;
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          30..209
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   ACT_SITE        136
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         39..41
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         92
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         117..120
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         134
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   SITE            172
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ   SEQUENCE   219 AA;  23171 MW;  BED6B8AB7704B5BD CRC64;
     MPDSADHSDP GGSLQWPLPQ PLPVAEAPLR LAVMASGAGT NLEALARACG EGRLHGQVVV
     LAVNRADCGA RARAERLGIP CQVLDHRHQP SREALDGALI RLFEAHRVDL VVMAGWMRIV
     TPVLIEAFPE RLVNIHPSLL PSFRGADGVG QALAAGVTLA GCTAHLVTAE VDAGPILVQA
     AVPVLAGDDR ERLHARIQHQ EHRILPLAVS LAARRLAQG
//
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