ID A0A093T4L5_PHACA Unreviewed; 1000 AA.
AC A0A093T4L5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3 {ECO:0000256|RuleBase:RU363089};
DE Includes:
DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|RuleBase:RU363089};
DE EC=6.3.4.13 {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|RuleBase:RU363089};
DE Short=GARS {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|RuleBase:RU363089};
DE Includes:
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|RuleBase:RU363089};
DE EC=6.3.3.1 {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=AIR synthase {ECO:0000256|RuleBase:RU363089};
DE Short=AIRS {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|RuleBase:RU363089};
DE Includes:
DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|RuleBase:RU363089};
DE EC=2.1.2.2 {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|RuleBase:RU363089};
DE AltName: Full=GAR transformylase {ECO:0000256|RuleBase:RU363089};
DE Short=GART {ECO:0000256|RuleBase:RU363089};
DE Flags: Fragment;
GN ORFNames=N336_00678 {ECO:0000313|EMBL:KFW89574.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW89574.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW89574.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW89574.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|RuleBase:RU363089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000256|RuleBase:RU363089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC Evidence={ECO:0000256|RuleBase:RU363089};
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, ECO:0000256|RuleBase:RU363089}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005174,
CC ECO:0000256|RuleBase:RU363089}.
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, ECO:0000256|RuleBase:RU363089}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family.
CC {ECO:0000256|ARBA:ARBA00008630, ECO:0000256|RuleBase:RU363089}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC {ECO:0000256|ARBA:ARBA00007423, ECO:0000256|RuleBase:RU363089}.
CC -!- SIMILARITY: In the central section; belongs to the AIR synthase family.
CC {ECO:0000256|ARBA:ARBA00008696, ECO:0000256|RuleBase:RU363089}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL423351; KFW89574.1; -; Genomic_DNA.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000053238; Unassembled WGS sequence.
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-UniRule.
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-UniRule.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd08645; FMT_core_GART; 1.
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 HAMAP; MF_00741; AIRS; 1.
DR HAMAP; MF_00138; GARS; 1.
DR HAMAP; MF_01930; PurN; 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; IPR004607; GART.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR InterPro; IPR000115; PRibGlycinamide_synth.
DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR InterPro; IPR020559; PRibGlycinamide_synth_CS.
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 NCBIfam; TIGR00877; purD; 1.
DR NCBIfam; TIGR00878; purM; 1.
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; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF01071; GARS_A; 1.
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.
DR PROSITE; PS00184; GARS; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363089};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU363089};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363089};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW ECO:0000256|RuleBase:RU363089};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|RuleBase:RU363089};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238}.
FT DOMAIN 113..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW89574.1"
FT NON_TER 1000
FT /evidence="ECO:0000313|EMBL:KFW89574.1"
SQ SEQUENCE 1000 AA; 106461 MW; D2AB17AA18D8049B CRC64;
RLMADRVLVI GSGGREHALA WKLAQSPHVK HVFVAPGNAG TADNGKISNS AVSVSNHAAL
AQFCRDQEVR LVVVGPEVPL AAGIVDDLTA AGVSCFGPTA KAAQLESSKS FTKAFLDRHE
IPTARWKSFT DPKAACSFIN SANFPALVVK ASGLAAGKGV IVASNKEEAC KAVTEIMQDK
AFGTAGETVV VEELLEGEEV SCLCFTDGVT IAPMPPAQDH KRLMDGDEGP NTGGMGAYSP
APQISKDLLQ KIRDTVLQKT VDGMRKEGVP YFGVLYAGLM LTKDGPKVLE FNCRFGDPEC
QVILPLLKSD LYEVMQAVIN KKLSSSMPIW YEDSAAVTVV MASEGYPGSY PKGLEITGLS
KAKQLGLEVF HAGTSLKDGK VVTSGGRVLT VTAIKEDLMT ALQEANKGVA AIHFKGAIYR
KDIGYRAIAF LRQSRGGLTY KNSGVDIAAG NTLVQKIKPL AAATSRSGCN AELGGFAGLF
DLKAAGYEDP ILVSGTDGVG TKLKIAQVCK RHDTIGQDLV AMCVNDILAQ GAEPLFFLDY
FACGKLDVEV AQSVIAGIAE ACKKAGCALL GGETAEMPGM YPPGEYDLAG FAVGAVERGQ
MLPQLERIAD GDVVIGVASS GVHSNGYSLV RKIVEKSSFD FSSPVGVSGD QTLGDLLLTP
TKIYSKTLLP VLRSGHVKAY AHITGGGLLE NIPRVLPESF GVFLDALTWK IPEIFCWLHK
EGNLSEEEMT RTFNCGIGAV LVVQKELAQQ VLKDIQRHEA AWMIGKVVSL QKGSAPVKVH
NMLRALQANR SLSLHSHIQG KIQTNKVKVA VLISGTGTNL EALINSTKKP TSFAQIVLVV
SNKAGVEGXX XXXTRVIDHK LFESRTEFDS AVDKVLEEFS VELICLAGFM RILSGPFVKK
WDGKILNIHP SLLPSFKGAN AHKLVLEAGV RVTGCTVHFV AEEVDAGAII FQEAVPVKVG
DTVETLSKRV KEAEHRAFPA ALQLVASGAV QVGEAGKIYW
//
