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
//