ID A8XSV0_CAEBR Unreviewed; 1337 AA.
AC A8XSV0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
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};
DE Flags: Fragment;
GN Name=pfas-1 {ECO:0000313|WormBase:CBG18026a};
GN ORFNames=CBG18026 {ECO:0000313|EMBL:CAP35553.1,
GN ECO:0000313|WormBase:CBG18026a}, CBG_18026
GN {ECO:0000313|EMBL:CAP35553.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP35553.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP35553.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP35553.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR EMBL; HE600963; CAP35553.1; -; Genomic_DNA.
DR RefSeq; XP_002642085.1; XM_002642039.1.
DR STRING; 6238.A8XSV0; -.
DR GeneID; 8584080; -.
DR KEGG; cbr:CBG_18026; -.
DR CTD; 8584080; -.
DR WormBase; CBG18026a; CBP39592; WBGene00037523; Cbr-pfas-1.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; A8XSV0; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000008549; Unassembled WGS sequence.
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:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 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:UP000008549}.
FT DOMAIN 41..148
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 175..223
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 437..593
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 852..987
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT NON_TER 1337
FT /evidence="ECO:0000313|EMBL:CAP35553.1"
SQ SEQUENCE 1337 AA; 148073 MW; B56909E3A86D1312 CRC64;
MTKFHVKLYS KAVESRKVSQ IQRDFEKKFH RKLDVSVEYC YHLIVDEPDF IDTNWSKLSN
LLSHSPFEKY VWRESILNSK NGKVIEICPR TAVKTATCTN ILNVFDSADI RNVEKIERGI
RYLVPNDVDE NDFFELAADK MTEVIYSTDM NFDNESHSIE NVTIIDVLAS KQNLIEANEK
LGLALDQDDL DFYYDFFVIK VKKNPTDVEL FDLAQSDSEH SRHWFFRGEI WIDACEREQS
LMGSIRDTLK YSNENSLIAF NDNSSSIRGF ERVWRLRPSD PTTVSSMNAI CSSSHLIYSA
ETHNFPTAVC PFQGATTGTG GRIRDVHATG RGAYEIAGTV GYSFGNLNIA GLDLPWEDPS
FVYPTSISEP AKIAIEASNG ASDYGNKFGE PVICGFARSF GLKLENGERC EYLKPIMFSG
GIGTIDEDEV KKEPCAVGQK VVKIGGPVYR IGVGGGAASS VSVQGNRENQ LDFAAVQRGD
AEMGGKLHRV VRACAERNGG NPLTSIHDQG AGGNGNVIKE LVEGCGVTVQ SDAFQLGDES
ISLRELWTAE YQENDAALVN PSLLEALQTI SEREKCHVSV VGDVMEEQRV KLVGKSGEIA
VDLDTRQLGE REKKCFKLKS VPRILKKLEL PKNLTVREAV GRVLKLPTVA SKRYLTCKVD
RSVTGLVAQQ QCVGPLHTPL ADVAVVALSH FDTVGGAVSL GEQPIKMLID AEKGARMCIS
ETIMNLIWAP ITDLKVSKTR YSKKKLFLLK DVKMSGNWMW AAKCEGEGAR LVEAVGGLCQ
GLREIGCAID GGKDSLSMAV TANGEVVKSP GTLVLSAYAP CTNVSKVVNP SLKATPGSKI
LWIKCGGVKG KFRLGGSALA QVYSQIGDDC PDIENFSEIS HVFSIVQDLL NEDQLVGTVR
KPKILAGHDI SDGGLITTIL EMAFAGNVSI DIDIQKETDP INILFSEECG IVLEVSDAEN
VMKRCQSSVI ECSVIGHATP EYGSDAHVKI QVNGKMEINE KLVDLREEWE LVGDKLGEHQ
TNLKSLEEAK NVRKDCKKIQ YKCDFEWFYH PSFIYHEQYF STAPRVAIIR EEGSNGDREM
ASAFTLAGFQ TFDVTMSDML KGHNLNSYRG VAFVGGFSYA DVLGSAKGWA AGIQFNEKVS
QSFKVFRSRS DTFSYGVCNG CQLMAQLGWV GDEDDESESV TVFLDENECG RFESNFGPVK
IEQSRCIMLS GMENSILGLW SSHGEGQFNY RSSQNLENLR RNGQVCVRFC DDLGMTGADY
SKEKLPYPWN PNGSIDDVAA ICSRDGRHLA MMPHADRSFL TWQWADPDDV NWNTRFDQQS
VALSPWIRMF RNAYNWC
//
