ID U3JI50_FICAL Unreviewed; 914 AA.
AC U3JI50;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00013047};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002454.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002454.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002454.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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; U3JI50; -.
DR STRING; 59894.ENSFALP00000002454; -.
DR Ensembl; ENSFALT00000002466.2; ENSFALP00000002454.2; ENSFALG00000002352.2.
DR eggNOG; KOG0237; Eukaryota.
DR eggNOG; KOG3076; Eukaryota.
DR GeneTree; ENSGT00390000000292; -.
DR HOGENOM; CLU_005361_0_2_1; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000016665; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-EC.
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:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
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; PF01071; GARS_A; 2.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01209; GARS_A; 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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 111..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 180..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 97720 MW; 877D61CEF2D32FDD CRC64;
MAERVLVIGS GGREHALAWK LAQSPHVKHV FVAPGNAGTA DSGKISNSAV LVSNHTIVTQ
FCKDHNIGLV LVGPEALLEA GIVDDLRAAG VRCFGPCARA AQLASNSSSS RAFLERHGLP
TARWRAFSSP QEACRFITST DFPARVLRAR GPAARKEVTI AASKEEACRA VQDIMQVDRN
TLPSPGCQPS LLGRQGSEPS ILPPPGRAAP GLGQPRTARA PQPSAGAGAA AALSFGSQVP
EALLEHIRAA ILQHIVDSLR QEGAAYVGVL QAGLMLTKEG VKILNFKCQF GDPQCQAILP
LLKNDFYEVI QAAIDGKLCS CMPAWSENRT AVCVVMASPG YPGDSDKGME VTGLLQAEAL
GLQVFHGGTA LKDGRVVTSG GRVLSITAVR QDLMEALGEA NRGVATIHFQ GATFRRDIGH
RGLRLLQQAG RTGKNLGIPS EFWSVLCLCL AGGPSGGGFA AFFDLKASGY HDPILVSQTK
GLGPKLQVAQ LCKRHDTIGQ DLVALCVNDL LAQGAEPLFF LTHLACGKLD AEVMETIKEG
IAEACRSAGC AFLGMDPPLL GDLKGLRLNL SPEKWIWEVE AECGPGIVGF CLVEKPVEIL
CFNFSLSVRW VSTEKWDALL TPGELFSPAL LPILRSGHVK GFAPTAEGLL GGVSRLLPEH
LGAVLDALSW KIPEIFCWLY KEGNLSAQEM AQTFPCGIGA VLVVQKELAQ HVLQDIQRQQ
EAWLIGKVVA PCDTGSHIEV ENLAEALQLS SPQQLLDDSS AEIQPQPGKR KVKVAVLVSG
AGELPLVLAQ RLSLHTRRGW ASSAHLAFYP MGSPDPSKPR VIDHKLYGSR SEFDSTIDRV
LQEFSVELIC LSGFMRVLSS SFLRKWKGKI LNASPSLFPL IKDGNAHQES PESEFKVTGC
TVHFVLVSGL RTGN
//
