ID M3VX22_FELCA Unreviewed; 1475 AA.
AC M3VX22;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 24-JAN-2024, entry version 67.
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};
GN Name=PFAS {ECO:0000313|Ensembl:ENSFCAP00000001542.4,
GN ECO:0000313|VGNC:VGNC:68800};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001542.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000001542.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001542.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000001542.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001542.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000001542.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001542.4};
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 EMBL; AANG04000740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000001542; -.
DR PaxDb; 9685-ENSFCAP00000001542; -.
DR Ensembl; ENSFCAT00000001662.6; ENSFCAP00000001542.4; ENSFCAG00000001662.6.
DR VGNC; VGNC:68800; PFAS.
DR eggNOG; KOG1907; Eukaryota.
DR GeneTree; ENSGT00390000007600; -.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; M3VX22; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000011712; Chromosome E1.
DR Bgee; ENSFCAG00000001662; Expressed in adult mammalian kidney and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IBA:GO_Central.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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; IPR040707; FGAR-AT_N.
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 InterPro; IPR036604; PurS-like_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; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 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 SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000011712}.
FT DOMAIN 219..295
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 323..371
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 583..740
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 1014..1121
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1295
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1475 AA; 159210 MW; 1A9F311311F8D02B CRC64;
MGIEEGTFWD EHWVLYGNQF VNKFHIKKKQ KKPQKTKTKP PKPRTQPITE LHKLEGCGGG
GGGGGGEVPE VLGGPAHGSE PRLFRAPRAG FLSITSGPGI VDSTCVWLSR VSPDTLFATP
FRHPLQEPNS SLQYGTPAEM PSVLHFYVRP SGHERAASGH TRRKLQGKLP ELQAVKTELC
YNVNWTAESL PSAEEMKKLT WLFGCPLLPG DVAQESWLRS DSSDLLLEVG PRLNFSTPAS
TNVVSVCWAA GLGAVDRVET TRRYLLSFAK PPSSETKTLA LATLHDRMTE QHFPQPIQSF
YLQSMSAPLN GQIDILAEGR RALEKANREL GLALDSWDLD FYTKRFQELK RNPSTVEAFD
LAQSNSEHSR HWFFKGQLHV DGQEMTHSLF EAIMSTQASS NPNNVLKFCD NSSAIQGKEV
RFLQPEDPTR PSCFRQQRAL RHVVFTAETH NFPTGVAPFS GATTGTGGRI RDVQCTGRGA
HVVAGTAGYC FGNLHIPGYN LPWEDPSFQY PENFARPLEV AIEASNGASD YGNKFGEPVL
AGFARSLGLQ LPDGQRREWI KPIMFSGGIG SMEAEHVSKE PPEPGMDVVK VGGPVYRIGV
GGGAASSVQV QGDNSSDLDF GAVQRGDPEM EQKMNRVIRA CVEAARGNPI CSLHDQGAGG
NGNVLKELSD PAGAVIYTSR FQLGDPTLNA LEIWGAEYQE SNALLLRPVD RDFLSRVSAR
ERCPACFVGT ITGDRRMVLV DDRDCPVGRN GEGDAPSPPT PVDLELDWVL GKMPRKEFFL
QRSVPVLRPL ALPPGLSVHQ ALERVLRLPA VASKRYLTNK VDRSVGGLVA QQQCVGPLQT
PLADVAVVAL SHQELVGAAT ALGEQPVKSL LDPKVAARLA VAEALTNLVF ALVTDLRDVK
CSGNWMWAAK LPGEGAALAD ACAAMVAVMA ALGVAVDGGK DSLSMAARVG SETVRAPGSL
VISAYAVCPD ITATVTPDLK RPGGRGRLLF VPLSPGQHRL GGTALAQCFS QLGEQPPNLD
LPENLVRAFR ITQGLLRDRL LCSGHDVSDG GLVTCLLEMA FAGNCGIEVD VPAPGVDALP
ALFAEEPGLV LEVRGPDLAQ VLKRYRDAGL HCLELGATGD AGPHALVRVS VNGAVVLEES
VRQLRALWEE TSFQLDRLQA EPRCVAEEEQ GLRERTGPTY CLPPGFPKAS VPREPGGPTP
RVAILREEGS NGDREMADGF HLAGFEVWDV TMQDLCSGAI GLDTFRGVAF VGGFSYADVL
GSAKGWAAAV TFHPLAGAEL RRFRKRPDTF SLGVCNGCQL LALLGWVGGS PSEEAEGTGQ
DSWPARPGLL LRHNLSGRFE SRWASVRVGP GPALMLRGME GAVLPVWSAH GEGYMAFSSP
ELQAQIEARG LAPLHWADDD GNPTEQYPLN PNGSPGGVAG VCSLDGRHLA LMPHPERAVR
LWQWAWQPPP FDTLTTSPWL QLFINARNWT REGGC
//
