ID A0A194RFG4_PAPMA Unreviewed; 736 AA.
AC A0A194RFG4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Trifunctional purine biosynthetic protein adenosine-3 {ECO:0000313|EMBL:KPJ16563.1};
GN ORFNames=RR48_08154 {ECO:0000313|EMBL:KPJ16563.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ16563.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ16563.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ16563.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ16563.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004686}.
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; KQ460211; KPJ16563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194RFG4; -.
DR STRING; 76193.A0A194RFG4; -.
DR InParanoid; A0A194RFG4; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
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 CDD; cd02196; PurM; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, 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 InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR NCBIfam; TIGR00639; PurN; 1.
DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240}.
FT DOMAIN 86..132
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 253..319
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 317..457
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 486..716
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
SQ SEQUENCE 736 AA; 79476 MW; 6B638364B1D83CB1 CRC64;
MVLIVEPGHV EELLAMVEDP IDVIGVVEAM GKEGGHQVVV EKFQQAMEPL RAPYSGTPPL
QKALSYKDSG VDIEAGDSLV SLIKPLARRV VAGIADGCRQ ANAALIGGET AEMPGMYPPG
VYDIAGFALG VVERSHILPK INDITELLAM VEDSIDVIGV VEAMGKEGGH QVVVEKFQQA
MEPLRAPYSG TPPLQKALSY KDSGVDIEAG DSLVSLIKPL ARSTTRSGVI GGLGGFGGCF
QLKAIEHEYK DPVLVVAADG VGTKLQVAQR ANRHDTIGLD LVAMCLNDIL CNGARPLTFL
DYFACGALDV NVARRVVGDI IIGLPSNGVH SNGFSLIHKL MKKAGLTLED KAPFSKEGLT
LGEELIKPTR IYVESVLPAL QRGAVKAVAH VTGGGLLDNL PRVIPDSVRA RLNAHWWHVH
PVFAWIADTG SVKDEEMLRT FNCGIGMVLI VSPEDQADER QWLRGFVDNF ASALDFTRRM
PLLNNKRVAV LVSGNGSNLQ ALVEASREPA HCMYADVALV ISNKPDAYAL KRAEAAGIPA
LVMNITRSFG AMVIGSIQAR PAGGARVLVD NFASALDFTR RMPLLNNKRV FNHKEYSSRE
EFDRAVSGAL ETHRIDLVCL AGYMRILSAE FVEKWKGRLV NIHPSLLPRH PGLHAARQCL
AAGDADSGCT VHFVDAGVDT GPIITQERVP VLKDDTEESL TERIHQAEHR AYPRALRLLA
TGRVRLSSEG EVLFHS
//