ID G0SH82_CHATD Unreviewed; 306 AA.
AC G0SH82;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=phosphoribosylglycinamide formyltransferase 1 {ECO:0000256|ARBA:ARBA00012254};
DE EC=2.1.2.2 {ECO:0000256|ARBA:ARBA00012254};
GN ORFNames=CTHT_0069060 {ECO:0000313|EMBL:EGS17571.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17571.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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}.
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DR EMBL; GL988047; EGS17571.1; -; Genomic_DNA.
DR RefSeq; XP_006697189.1; XM_006697126.1.
DR AlphaFoldDB; G0SH82; -.
DR STRING; 759272.G0SH82; -.
DR GeneID; 18260944; -.
DR KEGG; cthr:CTHT_0069060; -.
DR eggNOG; KOG3076; Eukaryota.
DR HOGENOM; CLU_038395_0_1_1; -.
DR OMA; IECREDE; -.
DR OrthoDB; 5621at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
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; IPR015915; Kelch-typ_b-propeller.
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 Pfam; PF13418; Kelch_4; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
PE 3: Inferred from homology;
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGS17571.1}.
FT DOMAIN 87..291
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
SQ SEQUENCE 306 AA; 33687 MW; 0F46F57B2289C27E CRC64;
MAANNTNGTI CVHGDCPSTG RLDDVWVFDV TSQTWTELPA APPPARGDLR LPLSARSCIA
CTGTTASESK AARSFGSALH AMADPCRIVV FASGNGSNFQ ALIDAVKDGR IPNSKIIRLI
VNRAKAYATT RADNAGIPWE YFNLISHGFQ AKGEQDPVKI QEARNKYDAA LAEKLLKGDY
KPELVILAGW MYVFGKAFLD PLEAAGIKII NLHPALPGKY DGAGAIERAY QDFKAGRLEN
NRTGIMVHYV IDQVDRGEPI LVREIECRED EDLHQLEERI HKNEHELIVE AAALVVKQIL
EQRSRQ
//
