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Database: UniProt
Entry: M2VWH0_GALSU
LinkDB: M2VWH0_GALSU
Original site: M2VWH0_GALSU 
ID   M2VWH0_GALSU            Unreviewed;      1439 AA.
AC   M2VWH0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ORFNames=Gasu_48850 {ECO:0000313|EMBL:EME27591.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME27591.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
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; KB454530; EME27591.1; -; Genomic_DNA.
DR   RefSeq; XP_005704111.1; XM_005704054.1.
DR   STRING; 130081.M2VWH0; -.
DR   EnsemblPlants; EME27591; EME27591; Gasu_48850.
DR   GeneID; 17086484; -.
DR   Gramene; EME27591; EME27591; Gasu_48850.
DR   eggNOG; KOG1907; Eukaryota.
DR   OMA; LSANWMW; -.
DR   OrthoDB; 2891567at2759; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
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   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, ECO:0000313|EMBL:EME27591.1};
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:UP000030680}.
FT   DOMAIN          133..254
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          283..330
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          548..704
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          972..1101
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1396
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1398
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1439 AA;  161784 MW;  6A26FC240D82718D CRC64;
     MAYDGKTSAR VAFGFQYDVV SLKTCTRKSG QSCTLFGLVT RFRLQSTQSF FLGSRKVPRH
     LHTLEQSRFD HYGPAMNLQE TKSQSNIATS QQNTGTFQRL YRSHQKDLEL LNRALLQCAV
     RKELPPIVNI KQEYCFYIQF SRKPSQEEEK RLYWLLSDPL YENSLSERSF FPSDEGSHPC
     FSLEIGPRLN FQTAWSSNAV TICQSCGLSC IERIERSKRY FLEWDNCDKE TLQPIMEQFT
     NTIHDRMTEM VYSSPLQSFE TPERAAPIQM VPLKEKGMTA LIELNQLLGL GLDEWDMKYY
     YDMFVNDLKR NPTVVELFDI AQSNSEHSRH WFFKGRIFLN GEEMSSSLLD MVRETWQKSP
     HPSVLAFCDN SSSIMGDSQC WMWSPEKPGK SLLSFPSKLT PNVQTMDITC TAETHNFPCG
     VAPFPGAETG SGGRIRDMSA TGVGSLVIAG TAGYSVGNLN LPDEQFDWED KSFSYPNHLA
     SCLKILIEAS NGASDYGNKF GEPLIAGFTR SFGMRLLNGE RREYIKPIMF SGGIGQMQHR
     HAYKESPQVG MLVVKIGGPA YRIGMGGGAA SSMYQGENKE ELDFGAVQRG DAEMEQKTYR
     VIRCCVELGE NNPIVSIHDQ GAGGNCNVVK ELIYPSGARI DIRKLWIGDK TLSVLELWGA
     EYQEQYGLLI RPDSKELFSN ICARENVTAS YIGTIDGSGR IVVFDSETQQ TAVDMELERV
     LGKLPQKCFY DEFIETECLK PLNMSFLSRD EWQRYNANEK KSIFMKVFER ILRLPSVGSK
     AFLTNKAMKY SMSFEIFEMA YIKLGPLQLP LADCAVVAMS YFGETGIVTA IGEQCIKSLL
     SPAAMARMAV AEMVTNLAGC KITSLSSIRC EANWMWPAKM PGEGANLYQA VRSLRDMLLS
     LGIAVDGGKD SLSMATKVVS SENESQLVKA PGTLVLSGYA FVPNIRKKVT PDIKRPGTSG
     ILYIDLAHGK RRLGASAFSQ VHKQLGDECP DLDDFLLLKR AFDAVQSLIE QGKVLSYHDV
     GEGGLLTALA EMAMAGNCGL DICFANQQHS PFAFFFAEES GMLIEVEDHQ LEFILIQLHG
     EQLPCWLAAI TTNDFKIQIQ YNGESLMERD IRDIRSIWDS TSFQLEKLQA DVSCAVAERK
     NRWLQTGPRY HLTFQPQMTS SAILHSSRKH KVAVIRVEGT NGDRELAVAF HLAGFEVWDV
     HMKDIENASV SLDSFSGVAF PGGFSFADVL DSSKGWAGII RYLPQVRAEF QRFYNRKDTF
     SLGVCNGCQL MAWLGWIPNH TDTIVVDSSQ ALFIQNKSGR FESRFSSVKI LPSVSIMLRG
     MEDSVLGIWC AHGEGQTVFT SESYYEQVVK LGLAPIRYVD DEGIPTEDYP WNPNGSRQGI
     AALCSMNGRH LALMPHPERV VFPWQWSYYP ETFPQDTSPW IRMFQNAREW CEQQKHSFT
//
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