ID A0A2P5ABY7_PARAD Unreviewed; 312 AA.
AC A0A2P5ABY7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=phosphoribosylglycinamide formyltransferase 1 {ECO:0000256|ARBA:ARBA00012254};
DE EC=2.1.2.2 {ECO:0000256|ARBA:ARBA00012254};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|ARBA:ARBA00041682};
DE AltName: Full=GAR transformylase {ECO:0000256|ARBA:ARBA00041324};
GN Name=PanFMT2A {ECO:0000313|EMBL:PON34031.1};
GN ORFNames=PanWU01x14_347700 {ECO:0000313|EMBL:PON34031.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON34031.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00036742};
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}.
CC -!- SIMILARITY: Belongs to the GART family.
CC {ECO:0000256|ARBA:ARBA00038440}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PON34031.1}.
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DR EMBL; JXTB01000684; PON34031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5ABY7; -.
DR STRING; 3476.A0A2P5ABY7; -.
DR OrthoDB; 974at2759; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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 InterPro; IPR001555; GART_AS.
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.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PON34031.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..284
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
SQ SEQUENCE 312 AA; 34376 MW; 0D00159F3133F3C7 CRC64;
MGANSMLSRF CSNIRISSIQ STKTLFSVTL LPPPLPSTPS FAQSHKWVSF RFSPCILLRD
SNRNTGACQN SASVQVVGMS SAEDLGIGLK RKKLAVFVSG GGYNFRSILK ASLQGSIFGD
IVVLILCSFC ILSFMVGCGG AEFVREKGIP IILFPRIKDE IDGVSPTNLV ATLRGFEVDF
VLLARYLKLI PAELIRAYPK SILNINPSLL PAFGGKGYYG MKVHKAVIAS GARFSGPTIH
FVDEHYDTGR ILAQRVVPVS PNDTPEDLAA RVLQEEHRLY VEVVEAICED RITWRQDGVP
LIRRKENPNE FR
//
