ID A0A176W4C9_MARPO Unreviewed; 1440 AA.
AC A0A176W4C9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AXG93_2015s1190 {ECO:0000313|EMBL:OAE27392.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE27392.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE27392.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE27392.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAE27392.1}.
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DR EMBL; LVLJ01001907; OAE27392.1; -; Genomic_DNA.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000077202; 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:UP000077202}.
FT DOMAIN 146..267
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 294..343
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 555..711
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 966..1100
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1440 AA; 156134 MW; 189A2FC6E22D126C CRC64;
MVGMATLALL PTARPTPAAG AVAERSAVSS RAHNSVRVLA GPVKSERALA SARALFKGKN
AGQSELFGDV VLVKLPEASK RPFSKICATL ASKESLQAKS ESVGGIDTKV QHLYRQPFLA
ENATEALLRL VKQKVSGDVE SIKTEQCYNI ALRAPISREK QDVLTWLLRE TYEPDQLQAS
SFLDSQNATG GNGVVVEVGP RLSFTTAWSA NAVSIFSACA LPEVSRIERS RRYLLSVRDG
AAPLDQDQLE KFAELVHDRM TECVYYSKLE TFETDTVPEP VIECPVLEKG RAALEEINIR
MGLAFDDFDL EYYTNLFQND MKRNPTNVEL FDIAQSNSEH SRHWFFKGEL ILDGQPAPKN
LMDLVKDTLR ENPNNSVIGF NDNSSAIRGR VVEPLRPSAP GTPSPLSTIK RDLDILFTAE
THNFPCAVAP FPGAETGAGG RIRDTHATGI GSLIGASTAG YCVGNLQMED SFAPWEDNSF
EYPSNLASPL QILLDASDGA SDYGNKFGEP LIQGYTRTFG MRLLNGERRE WLKPIMFSAG
IGQIDHQHLK KEDPEVGMLV VKIGGPAYRI GMGGGAASSM VSGQNNAELD FNAVQRGDAE
MSQKLYRVVR TCVEMGDKNP IVSIHDQGAG GNCNVVKEII YPKGAEIDVR AVVVGDKTMS
VLEIWGAEYQ EQDALLIRPE NESLLRSICA RERVSMAVLG SISGSGRVVL VDSEARKQAA
ASGLPEPRPA VDLDLEKVLG DMPRKNYHFT RAQPVLEALD IAPGSTVFDA LNRVFHLPSV
CSKRFLTSKV DRCVSGLVAQ QQTVGPLQLP LADVAVYSQT YTGISGGACS IGEQPLKGLL
DAKAMARLAL GESLTNLVWA KVTALKDVKA SGNWMYAAKL DGEGAAMYDA AEALREAMIA
LEVAIDGGKD SLSMAAQAGG ETVKCPGNLV ISSYVTCPDI TKTVTPDLKL GDEGVLLHID
LARGKRRLGG SALAQVYDQI GDVCPDVDIH HLKAAFNAVQ VLLDRRAIAA GHDISDGGII
TALSEMAFAG NCGIVVDLPS PADDNSQLAP FSTLFAEELG LLLEVKRSDK DAILAELEAA
GVTCSAIGKV TSDPKIVVSV DGEVHVDKPT SYLRDLWEET SFTLEKLQRL ESCVEQEQQG
LKDRTTPTWE LSFTPSKTDE KYMNSTVKPK VAIIREEGSN GDREMSAMVL AAGFEPWDVA
MSDLLAGKAS LKDYKGIVFV GGFSYADVLD SAKGWAGTIR FNEVLLEQFQ EFYNRSDTFS
LGVCNGCQLM ALLGWVPGAD VGGTLGAGGD TAQPRFVHNE SGRFECRFSS VRIEKSPALM
LQGMEGTKVG VWVAHGEGRV LFPDAAIRDV IEKDSLAPIR YCDDSGEATE AYPFNPNGSP
QGIAALCSPD GRHLALMPHP ERCFMMWQFP WYPQEWSTLD RSGPSPWLKM FQNAREWCDQ
//
