ID A0A1D1UUE7_RAMVA Unreviewed; 1387 AA.
AC A0A1D1UUE7;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=RvY_05259-1 {ECO:0000313|EMBL:GAU93296.1};
GN Synonyms=RvY_05259.1 {ECO:0000313|EMBL:GAU93296.1};
GN ORFNames=RvY_05259 {ECO:0000313|EMBL:GAU93296.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU93296.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAU93296.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU93296.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAU93296.1}.
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DR EMBL; BDGG01000002; GAU93296.1; -; Genomic_DNA.
DR STRING; 947166.A0A1D1UUE7; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000186922; Unassembled WGS sequence.
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:UP000186922}.
FT DOMAIN 77..181
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 210..258
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 476..629
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 897..1022
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1211
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1387 AA; 152564 MW; 6870682A44C30898 CRC64;
MEDYTQAKKA HPAKEVLRFI NNSSWRAIPR SSLRLPEDVL PHVVSVRVQP VFYVEIDSNL
HKNDVEYRET IDQLRWLTES DFFKAAATNG HASHQAGENG WENGAEFEFQ VEIGPRLNFK
TPFCANALSI TAALSLHSVT RIERSSLCTI RYHAADSASS DYLKQACISH LMDPILQCEY
KSPITSFRVD LPKQQTFLVP VCKEGRTALA VANEQLSLGF DEADLDYYTH LFRTELKRDS
TNLECMDLAQ SNSEHSRHWF FNGKMVIDGK TIPATLFQMV KNTNLPQFTN PNNIIKFHDN
SSSIQGYDAL PLFRVTNPLS PSAFEKSPGT RHIIFTAETH NFPTAVEPFS GATTGTGGRI
RDVQAAGRGA HVIAGTVGYS FGSCYIPDFD APWEEQNATY PTNFARPLKV IIEASNGASD
YGNKFGEPVI TGFARSFGAT LPDGARCEWI KPIMFSGGIG SIDHQWTEKQ KELPNGMKVV
KIGGPVYNIG LGGGAASSTS VQGSNNSAVD LNAVQRGDAE MEQKLNRVIR ACIELEDNPI
VSIHDQGAGG NANVLKEIVD PAGALIKADQ FTLGDETVSI VALWNAEYQE SVAVLVPEDK
IDVLKSIAHR ERCTVDVVGE ITGTGKIVLE DFGKGRSQST DERINTPVDL PLELVLGDIP
RKTYHLERHH PRESKPELEQ RFRRSVAANF DMTKLQESLY RLLRLPSVGS KRYLTNKVDR
SVTGLVAQQQ CVGPLHTPLA DVAVIALCHF DTKGSATAIG EQPIKMLFDV KRGARMTVIE
SLTNLVFAKI SDLKDVKCSA NWMWPAKLPG EGAALFDACQ AMCGIMKELG IAVDGGKDSL
SMAAKCGDEI VKSPGTLVVS TYVQCPDIRK VITPSLRVPG GKGCLLWIDP GRGHRRLGGS
AYCQANSLLN IPFEAPDVDS VDTFVRAFQL TQRFLDGGKL SAGHDISDGG LIVCLLEMAI
AGNCVFDVNI ETPGEFAPEY LLFAEEVGWV LEVPEEYCDT ISDSFSEAGV PCFFIGHSTK
SSEECRSANG RNFCAPFISM DNRLVFGAEK EGIAGIRSVW EEFSYHIEKL QTNEGCAESE
KAMLAAGADP IFHVSFTPDF DVCDIAAFDR DRHLPPKVAI IREEGSNGDR EMAATLHMVG
FEVWDVNVQD LLDEKIDLGP FRGLVFVGGF SYADVFGSAK GWAAVLAFSP SARKQLENFY
QREDTFSLGV CNGCQLLTKL GLVGHTSVQS NGAKHIDVND TPVQLKHNIS KRFESRFSTV
KITSSNAIMF RGMEGTQLGI WVAHGEGKFA FRDGTSGLKS ASCIALQYVD RRGIPTEVYP
LNPNGSPEGI AGICTPNGRH LVMMPHPERS VLAWQWPWRP EDFNWPKDAA FTPWIKMFRN
AYEWCLA
//
