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Database: UniProt
Entry: A0A8C7DSM1_NAJNA
LinkDB: A0A8C7DSM1_NAJNA
Original site: A0A8C7DSM1_NAJNA 
ID   A0A8C7DSM1_NAJNA        Unreviewed;       862 AA.
AC   A0A8C7DSM1;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 20.
DE   RecName: Full=phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00013047};
DE            EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
OS   Naja naja (Indian cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=35670 {ECO:0000313|Ensembl:ENSNNAP00000009521.1, ECO:0000313|Proteomes:UP000694559};
RN   [1] {ECO:0000313|Ensembl:ENSNNAP00000009521.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSNNAP00000009521.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A8C7DSM1; -.
DR   Ensembl; ENSNNAT00000009984.1; ENSNNAP00000009521.1; ENSNNAG00000005957.1.
DR   GeneTree; ENSGT00390000000292; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000694559; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:InterPro.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046084; P:adenine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd02196; PurM; 1.
DR   FunFam; 3.40.50.20:FF:000006; Phosphoribosylamine--glycine ligase, chloroplastic; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR   Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-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   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
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   InterPro; IPR011054; Rudment_hybrid_motif.
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; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694559};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          245..334
FT                   /note="Phosphoribosylglycinamide synthetase C-domain"
FT                   /evidence="ECO:0000259|SMART:SM01210"
SQ   SEQUENCE   862 AA;  94450 MW;  C2D36CA022EF6F0A CRC64;
     MADRVLVIGR GGREHALAWK LAQSPHLKQI LIAPGNAGTA DDGKMSNSGV LISNHTILSQ
     FCKDHNIGCV IAGPETLLAA GIVDDLVAAG IPCFGPTAKA AQLGTNRYFT NIFLDQHGIP
     TARWKAFSNP KEALAVLFIM QDNMCCHSGD SSDTVIIEEL LKGEEFSVCC FIKYLGQNHH
     CLLGLLFILI TYSNVIIYVC VYVCTHQRWY SIILQLLKSD LYEVIQAAIG GQLCSSILAW
     SDDCTAVSVS MENGSYLQGH KKSMEITGLL QANELGLEIF HGATIIKEGK VLSNGNRILT
     ATAVKQDIMS ALEDIYKGLA VVSIQGATYG KETSCPGHDG FISAFFDLKA SGYRDPILVS
     HAKGIGTKLK VAQLCNKHDM IGQDLVAICV NDLLVQGAEP LFFHGHFAFG KLDVGVAQLT
     QAVSDGIVEA CKLAGCTFLG RETNEMPATC AAGEYNLVGF AVGAVERSMK FPQQGNIVIP
     GGYGNHTLGE QLLTPTKIYS RALLPVARSG NVKAFIHIGW RIPTHHLYFL KKLISHTHKW
     KIPSVFSWLQ EEGNLSEEEM GQIFNCGIGA VLIVQREAAR KVLKDVQKHE DAWMIGKVVH
     RTAAYASSGY PQVEIKNLSE VLLQNKWPFL KDVSNADNPP HTIHRKHKVK VAVLISGTGT
     SLSALLAYAK EPASCSEVVL VIANRSGVEE LRNATLAGIP TRVIDHKLYG SRSEYEGTID
     SVLEEFSIEL ICLSGFIRIL SSNFLRKWYG KMLGTYPSVS PLSKRRNIYN QAHPSTDKIV
     GCTVHFVLET SPEAIIVQEP VCVKAEDTQE TLYAKIKEAE NHVFPMALQL VASGMVQLRG
     DGKTYWKRER QELICQKERQ DC
//
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