ID B7GU65_BIFLS Unreviewed; 1244 AA.
AC B7GU65; E8MM14;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:ACJ53011.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:ACJ53011.1};
GN OrderedLocusNames=Blon_1941 {ECO:0000313|EMBL:ACJ53011.1};
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=391904 {ECO:0000313|EMBL:ACJ53011.1, ECO:0000313|Proteomes:UP000001360};
RN [1] {ECO:0000313|EMBL:ACJ53011.1, ECO:0000313|Proteomes:UP000001360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [JGI]
RC {ECO:0000313|Proteomes:UP000001360};
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
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DR EMBL; CP001095; ACJ53011.1; -; Genomic_DNA.
DR RefSeq; WP_012578218.1; NZ_JDTT01000029.1.
DR AlphaFoldDB; B7GU65; -.
DR KEGG; bln:Blon_1941; -.
DR PATRIC; fig|391904.8.peg.2020; -.
DR Proteomes; UP000001360; Chromosome.
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; 1.
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; 1.
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 Ligase {ECO:0000313|EMBL:ACJ53011.1};
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 1084
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1244 AA; 134332 MW; E1FB5F8354AE70C5 CRC64;
MVFRVYVEKK PGFDVEAQQL AGELRTILGL NGLKALRIVN RYDVEGISQE LFDQTVPTVF
SEPQVDNVAY DLPDFAGAKV FATEFLPGQF DQRADSAAEC IQLISQGERP TVRSAKLYAL
EGDLTDADVD TIKHYVINPV EAREASLETK ETLKTQVPVP GKVETLTGFN EMDAEAGQRF
IDERGLAMDL ADLEFCQKYF SEEGREPTIT EIKVIDTYWS DHCRHTTFGT ELDEVTIDDA
TVKAAFERYL AMRHELGRDA KPVCLMDMGT IGAKWLKKNG ILTGLDESEE INACTVKVKV
DVNGHDEDWL FLFKNETHNH PTEIEPFGGA ATCIGGCIRD PLSGRSYVYQ AMRVTGAADP
TVPVSETLEG KLPQRKLVTT AAAGYSSYGN QIGLATGQVD EIYHPGYVAK RMEVGAVVAA
TPADHVRRET PAPGDKIILL GGRTGRDGIG GATGSSKAHN VESLELDGAE VQKGNAPVER
KLQRLFRRGD ACRLIKRCND FGAGGVSVAV GELADGLFVD LNTVPKKYEG LDGTELAISE
SQERMAVDVA AEDVDEFLAY AREENLEATV IATVTEDPRM VMTWNGDKIV NLSREFLASN
GASKHQTVHV EAQQSYETPW GEGTLAERMN ELVTDINVAS NKGLSERFDS TIGAGTVLMP
FGGKRQLTPN MAMVAKLPVF GETTTASAMA WGFNPYIMSK NQFTGAYLSV VESLAKLVAA
GFEHEKAYLS FQEYFEKLRD EPERWGKPAA AVLGALMAQV DLGAGAIGGK DSMSGSFEDL
DVPPTLISFA VAVGNMKRAT SPEFKDADHR IVRIAPRYLA DGLTPDKDAL LEAFSVIEEL
TDFHDALAVS TPGYGATAEA LFKMTLGNRI GVTLNNSIAV DDLFTPAYGS FIVELADDAK
LPAVSNLVEI GEIGTTTSEY VFKAAGETLD LDAVQEAWES GIESVFPYRS KGEDKGATVE
TIDFHAPKKT VYVGSSVAKP HVVIPVFPGN NCEYDSAAAF ERAGADVTTL IVNNLTPAAV
AESTQALVDE INKSQIVMIP GGFSGGDEPD GSAKFITAFF RAPAVTEAVR DLLKNRDGLM
LGICNGFQAL VKLGLVPYGD IVPMTDACPT LTFNTIGRHQ SRLVRTRVAS DLSPWLSKTS
VGDIHTVAIS HGEGRFVASD EVLAQLRANG QIATQYVDET GTPGMDLDVN PNGSLLAIEG
ITSPDGRVFG KMGHSERSGN GLYVNVPGNK YQPIFEAGVE YFAA
//
