ID A0A261FMN8_9BIFI Unreviewed; 1255 AA.
AC A0A261FMN8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:OZG60417.1};
GN ORFNames=BMYO_0878 {ECO:0000313|EMBL:OZG60417.1};
OS Bifidobacterium myosotis.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630166 {ECO:0000313|EMBL:OZG60417.1, ECO:0000313|Proteomes:UP000216871};
RN [1] {ECO:0000313|EMBL:OZG60417.1, ECO:0000313|Proteomes:UP000216871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100196 {ECO:0000313|EMBL:OZG60417.1,
RC ECO:0000313|Proteomes:UP000216871};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG60417.1}.
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DR EMBL; MWWW01000008; OZG60417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FMN8; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000216871; Unassembled WGS sequence.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; 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; IPR010141; FGAM_synthase.
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 NCBIfam; TIGR01857; FGAM-synthase; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 183..225
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 433..584
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1095
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1255 AA; 134771 MW; 114081D93CCE8F2A CRC64;
MVFRVYVEKK PGFDVEAQQL AGELRTILGL TGLKAVRIVN RYDVEGISEE LFRAATPTVF
SEPQVDDVSA DLPDFGDAKV FATEFLPGQF DQRADSASEC IQLISQGERP AVRSAKVYAL
EGDLSEADVE TIKHYVINPV EAREASLDVR ETLKTQVPTP GKVEVIAGFN EMDAAAGQRF
IDERGLAMDL ADLEFCQKYF AEEGREPTIT EIKVIDTYWS DHCRHTTFGT ELDEVDIDDA
VVKAAFDRYL AMRHELGRDA KPVCLMDMGT IGAKWLKKNG ILTGLDESEE INACTVKVKV
DVNGKDEDWL FLFKNETHNH PTEIEPFGGA ATCIGGCIRD PLSGRSYVYQ AMRVTGAADP
TVPVSQTLEG KLPQRKLVTT AAAGYSSYGN QIGLATGQVD EIYHPGYVAK RMEVGAVVAA
TPADHVRRET PAPGDKIILL GGRTGRDGIG GATGASKAHN VESLELDGAE VQKGNAPVER
KLQRLFRRGD ACRLIKRCND FGAGGVSVAV GELADGLYVD LNTVPKKYEG LDGTELAISE
SQERMAVDVA AEDVDEFLGY AREENLEATV IATVTENPRM VMTWNGDEIV NLSREFLASN
GASKHQTVHV EAQQAYEVPA EWRSGTLGER MHALVTNLNV ASNKGLSERF DSTIGAGTVL
MPFGGTKQLT PNEAMVAKFP VFGETTTASA MAWGFNPYIM EKNQFTGAYL SVVESLAKLV
AAGFEHEKAY LSFQEYFEKL RDEPERWGKP TAAVLGALMA QVDLGAGAIG GKDSMSGSFE
DLDVPPTLIS FAVAVGNMKR ATSPEFKGAG HRIVRIAPRY LADGLTPDKD ALLDAFALVE
ELTDPSHHTA LAVSTPGYGG TAEALFKMTV GNGIGVDLND GIAVDDLFAP AYGSFIVELA
DNEKIPAVSN LVEVGEIGVT TEDYAFRAAD ETIDLADLQN AWEGGIESVF PYRSKGDEQG
KTVETIDFHV SDSAEAGIRK TVYTGASVAK PRVIIPVFPG NNCEYDSAAA FERAGAEVST
LIVNNLTPAA VAESTAALVE EISKSQIVMI PGGFSGGDEP DGSAKFITAF FRAPAVTEAV
RDLLKNRDGL MLGICNGFQA LIKLGLVPFG DIVPMTAECP TLTFNTIGRH QSRLVRTRVA
SDLSPWLAKT SVGDVHTVAI SHGEGRFVAS DEVLASLKAN GQIATQYVSE AGVPGMDLAV
NPNGSMLAIE GITSPDGRVF GKMGHSERSG NGLYANVPGD KYQPIFEAGV EYFAA
//
