ID A0A3Q1J1K8_ANATE Unreviewed; 1317 AA.
AC A0A3Q1J1K8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000026795.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000026795.1}
RP IDENTIFICATION.
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 STRING; 64144.ENSATEP00000026795; -.
DR Ensembl; ENSATET00000027220.2; ENSATEP00000026795.1; ENSATEG00000018442.2.
DR GeneTree; ENSGT00390000007600; -.
DR InParanoid; A0A3Q1J1K8; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000265040; Unplaced.
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; 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; 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:UP000265040}.
FT DOMAIN 43..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 852..971
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1148
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1317 AA; 143513 MW; 448536B02F9BB914 CRC64;
MAVVRFYSNE AVQGRALQRA AKLYPQLSIT TELCYNVELT GCESLSEEQK EVLLWLFRPP
LQAEPLSEKP NLSAGSGERL VEIGPRLNFS TAWSTNAVSM CRSAGLTNVT RVELSRRFLI
KPQHGESTQD VNGDVKKLIE CLYDGMTECI YQHPITSFTV ETKPQPVFEV DILGNGRAAL
EAANDELGLA FDSWDLDYYT SMFQRIKRNP TSVECFDLAQ SNSEHSRHWF FRGRMVIDKQ
EQKETLFSLI MDTQQHSNQN NVIKFCDNSS GIKGMELDCV YPKDPSQASP YETRRSLRHV
IFTAETHNFP TGVAPFSGAT TGTGGRIRDV QSAGRGGHVI AGTAGYCFGN LHIPGYVLPW
EPEGEGWEYP SSFAPPLQVA IEASDGASDY GNKFGEPVLS GFARSFGMRL ANGERREWIK
PIMFSGGLGS IEDTHVKKEE AETGMEVVKI GGPVYRIGVG GGAASSVQVQ GDNSNDRDLG
AVQRGDAEME QKMNRALRAC LERSGGNPIC SIHDQGAGGN GNVLKELSEP AGAIIYCSRF
KKGDPTLSVL ELWGAEYQES NALLLQPADR SFLERVCQRE KCPVDFVGNI TGDGKIVLVD
DEGGSRDLAD RGRCPVDLQL DWVLGKMPQK EFRMERLTPT HQALTLPAGL TVKDALTRVL
RLPAVASKRY LTNKVDRSVT GLVAQQQCVG PLHTPLADVA VVALSPFSIE GVATAIGEQP
IKGLVCPAAG ARMAVGEALT NLVFARVTAL KDVKCSGNWM WAAKLPGEGA SLWEACKAMC
EVMGQLGIAI DGGKDSLSMA ARVGKETVKA PGALVISAYA VCPDITATVT PDLEDPDGKG
MLLWVPLSPG HHRLGGSALA QCYSQLGDCS PDLDKPYLLT SCFNTTQTLI HDRLLSAGHD
ISDGGLISCL LEMAFAGNRG IDVELSQGTG VMELLFSEEL GLVLEVSESH VKTVRQRYSD
AGVECHHIGR TCGFGPEAMV SVRVDGQEVL REKLPNLRAL WEDTSFQLER LQANELCVQQ
EKEGLAKRTQ PYFNLTFDPS ETPSIDQLSS GQPRVAVVRE EGSNGDREMS VSLYMAGFEV
WDVTMQDLCS GSLTLEQFKA VVFVGGFSYA DVLGSAKGWA ATVTYNPKAK AEFDRFWQRD
DTLSLGVCNG CQLLALLGWV GEGEDAAGSE VVLTHNESGR FESRFVSVGI EKSPSVWLRG
MEGSALGVWV AHGEGLMQFR SSQAKNRIIS GGLAPLRYLD DQGQPTEVYP LNPNGSPQGI
AGLCSRDGRH LAMMPHPERC TLGWQWPWAP RDFRASLKPS PWLRMFKNAA AWCSKTQ
//
