ID A0A2K5E6T0_AOTNA Unreviewed; 1227 AA.
AC A0A2K5E6T0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=phosphoribosylformylglycinamidine synthase {ECO:0000256|ARBA:ARBA00012747};
DE EC=6.3.5.3 {ECO:0000256|ARBA:ARBA00012747};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|ARBA:ARBA00032632};
DE AltName: Full=Formylglycinamide ribotide amidotransferase {ECO:0000256|ARBA:ARBA00029823};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000028859.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000028859.1}
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 1/2.
CC {ECO:0000256|ARBA:ARBA00004920}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608}.
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DR AlphaFoldDB; A0A2K5E6T0; -.
DR STRING; 37293.ENSANAP00000028859; -.
DR Ensembl; ENSANAT00000046885.1; ENSANAP00000028859.1; ENSANAG00000032144.1.
DR GeneTree; ENSGT00390000007600; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT DOMAIN 86..134
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 346..504
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1047
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1227 AA; 132445 MW; ABDB0E92927B287D CRC64;
LDDVSQSWLP SGSMTCCWQK SGPVKYLIPS FAHPPSAEME AIALATLHDR MTEQHFPHPI
QSFSPESIPA PLNGPINILG EGRLALEKAN QELGLALDSW DLDFYTRRFQ ELQRNPSTVE
AFDLAQSNSE HSRHWFFKGQ LHVDGQKLVH SLFESIMSTQ ASSNPNNVLK FCDNSSAIQG
KQVRFLRPED PTQPSRFRQQ QGLRHVVFTA ETHNFPTGIC PFSGATTGTG GRIRDVQCTG
RGAHVVAGTA GYCFGNLHIP GYNLPWEDPS FQYPGNFARP LEVAIEASNG ASDYGNKFGE
PVLAGFARSL GLHLPDGQRR EWIKPIMFSG GIGTMEAEHV SKEPPEPGME VVKVGGPVYR
IGVGGGAASS VQVQGVNTSD LDFGAVQRGD PEMEQKMNRV IRACVEAPDG NPICSLHDQG
AGGNGNVLKE LSDPAGAIIY TSRFQLGDPT LNALEIWGAE YQESNALLLR PPHRNFLTHV
SARERCPACF VGTITGDRRI VLIDDRECPV GRNGQGDAPQ TSPPTPVDLE LEWVLGKMPR
KEFFLQRSPP VLKPLALPVG LSVHQALERV LRLPAVASKR YLTNKVDRSV GGLVAQQQCV
GPLQTPLADV AVVALSHEEL VGAATALGEQ PVKSLLDPKV AARLAVAEAL TNLVFALVTD
LRDVKCSGNW MWAAKLPGEG AALADACEAM VAVMAALGVA VDGGKDSLSM AARVGTETVR
APGSLVISAY AVCPDITATV TPDLKHPEGR GHLLYVPLSP GRHRLGGTAL AQCFSQLGEH
PPDLDLPENL VCAFRCTLVP PTCLVTCLLE MAFAGNCGLW VDVSVPGVDV LSVLFAEEPG
LVLEVQEPDL AQVLKRYQDA GLHCLELGHT GQAGPYAMVR VSVNGAVVLE EPVGELRALW
EETSFQLDRL QAEPHCVTEE ERGLRKRMGP SYCLPPTFPK ASVPREPGGP SPRVAILREE
GSNGDREMAD AFHLAGFEVW DVTMQDLCSG AIGLDTFRGV AFVGGFSYAD VLGSAKGWAA
AVTFHPRAGA ELRRFQKRPD TFSLGVCNGC QLLALLGWVG GDPNEDATEM GPDSEPARPG
LLLRHNLSGR FESRWASVRV GPGPALMLRG MEGAVLPVWS AHGEGYMAFS SPELQAQIEA
RGLAPLHWAD DDGNPTEQYP LNPNGSPGGV AGICSRDGRH LALMPHPERA VRPWQWAWRP
PPFDTLTTSP WLQLFINARN WTREGSC
//
