ID H2MIR0_ORYLA Unreviewed; 1319 AA.
AC H2MIR0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-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:ENSORLP00000018543.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000018543.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000018543.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018543.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000018543.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018543.2};
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_004068232.1; XM_004068184.2.
DR STRING; 8090.ENSORLP00000018543; -.
DR Ensembl; ENSORLT00000018544.2; ENSORLP00000018543.2; ENSORLG00000014791.2.
DR GeneID; 101156076; -.
DR KEGG; ola:101156076; -.
DR CTD; 5198; -.
DR eggNOG; KOG1907; Eukaryota.
DR GeneTree; ENSGT00390000007600; -.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; H2MIR0; -.
DR OrthoDB; 2891567at2759; -.
DR TreeFam; TF106371; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001038; Chromosome 4.
DR Bgee; ENSORLG00000014791; Expressed in gastrula and 13 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:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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:UP000001038}.
FT DOMAIN 34..153
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 180..228
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 443..599
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 851..972
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1149
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1319 AA; 143386 MW; 2DD2F693C82179EC CRC64;
MAVVRFYSSE APDGRALQRA AKLFPHLTLT TELCYNVELT GRESLSAEEK EVLLWLFRPP
LQAEPLSENP NLIESSEEKL VEIGPRLNFS TAWSTNAVSI CRSAGLTNVT RVEVSRRFLV
KPKNGKGTGE LSGDMKKLID CLHDSMTECV YHRPITSFAV ETKRQPVFEV DILAKGRAAL
EKANDDLGLA FDSWDLDYYT SMFQRIQRNP TSVECFDLAQ SNSEHSRHWF FRGRMLIDGQ
EQKETLFSLI MDTQRHSNPN NVIKFCDNSS GIKGVEIECV YPKDPSRASP YETRLSLRHV
IFTAETHNFP TGVAPFSGAT TGTGGRIRDV QSAGRGGHVI AGTAGYCFGN LHIPGYELPW
ESAGEEWEYP SSFAPPLQVA IEASDGASDY GNKFGEPVLS GFARSFGMRL PNGERREWIK
PIMFSGGLGS IEDSHVKKEE ASPGMEVVKI GGPVYRIGVG GGAASSVQIQ GDNCSERDLG
AVQRGDAEME QKMNRALRAC LERSDGNPIC SIHDQGAGGN GNVLKELSEP AGAVIYSSRF
KKGDPTLSVL ELWGAEYQES NALLLHPSDR SFLESVCQRE KCPVDFVGNI TGDGKIVLVD
DEGGSNDQVD SVRHPVDLQL EWVLGKMPQK EFRLERVALA CQPLRLPAGL SVRDALQRVL
RLPSVASKRY LTNKVDRSVT GLVAQQQCVG PLHTPLADVA VVALSPFSLE GAATAIGEQP
IKGLVCPAAG ARMAVGEALT NLMFARVTAL KDVKCSGNWM WAAKLPGEGA YLWEACKAMC
KVMSELGVAI DGGKDSLSMA ARVGKETVKA PGALVISAYA VCPDISATVT PDLEDPDGKG
VLLWVPLSPG NHRLGGSALA QCYGQLADCS PDLDHAELLT ACFSTTQTLL QDRIVSAGHD
ISDGGLISCL LEMAFAGNRG IDIELSSQGS EVMELLFSEE LGVVLEVSEC DVEAVCQRYS
DAGVQCHRIG RTCGFGPKAE VRVCVDGQEV LKESLPELRA AWEDTSFQLE CLQANELCVK
QEEEGLAKRT QPYFQLNFDP SESPSVRRLA GGPPRVAVIR EEGSNGDREM SASLYMADFE
VWDVTMQDLC CGSLTLELFK AVVFVGGFSY ADVLGSAKGW AAAATYNAKA KAEFDRFQQR
EDTLSLGVCN GCQLLALLGW VGETADGAGS EVVLTHNRSG RFESRFVSVG IQESPSIWLR
GMEGSALGVW VAHGEGLMQF RSSMAQDLII SGGLAPLRYL DEQGFPTEEY PLNPNGSPQG
VAGLCSRDGR HLAMMPHPER CTLSWQWPWA PRELRPSLVP SPWLRMFKNA AAWCSNTDV
//
