ID A0A086BPH4_9BIFI Unreviewed; 1375 AA.
AC A0A086BPH4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:KFF31838.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:KFF31838.1};
GN ORFNames=BBOMB_1243 {ECO:0000313|EMBL:KFF31838.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31838.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF31838.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31838.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
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:KFF31838.1}.
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DR EMBL; ATLK01000001; KFF31838.1; -; Genomic_DNA.
DR RefSeq; WP_044087549.1; NZ_JDTS01000004.1.
DR STRING; 1341695.BBOMB_1243; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR Proteomes; UP000028730; 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; 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; 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 Ligase {ECO:0000313|EMBL:KFF31838.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000028730}.
FT DOMAIN 213..255
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 475..626
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1216
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1375 AA; 147696 MW; 9DE46CD13369C744 CRC64;
MVFRIYVEKK QGFEVKADQL LDEWRDVLGL DTLVAVRIVN RYDVDGVSEE LFQRAVRTVF
SEPQSDVTAT DLDALLEGMP MGTQEGGDGA VDVSGNGSYG SSSVRAVFAV EPLPGQFDQR
ADSAAECIQL ISQAGRPQVR TATIYVLEGS SLSQTDVQAV KRYVINPVES RETDVDAPVP
DTLQVRVPVP ADVERITGFN ELDDEGLRGF IRDRALAMDL GDIKVCQDYF RGEGRVPTIT
EIKVVDTYWS DHCRHTTFGT RLDDVRIDDA VVRRAFDEYL RMRRELKREG KPCSLMDIGT
IGAKWIKSLG GLESLDESEE VNACTVKVKV DVAAGGGHAG GAATKKETQD WLFLFKNETH
NHPTEIEPFG GAATCIGGCI RDPLSGRSYV YQAMRVTGAG DPRVPVGQTL PGKLPQRKLV
TAAAEGYSSY GNQIGLATGQ VSEIYHPGYV AKRMEVGAVV GATPADHVRR ETPSAGDRII
LLGGRTGRDG IGGATGASVA QDEHSLEERG AEVQKGNAIV ERKLQRLFRR KDACRLIKRC
NDFGAGGVSV ATGEIADGLC IDLDAVPKKY EGLDGTDLAI SESQERMAVD VAAKDVDEFL
RYAKEENLEA TVVAVVTREP RMRMTWRGDT IVDLSREFLA SNGAQKHQSV HIRADERTAS
GNDGDDVGGQ DILAYTHPWR MGSLSERLNA LVGDINVASN KGLAERFDST IGAATVLMPF
GGRRQLTPTQ AMVAKFPVEG ETDTASAMAW GFNPYISERN QYAGAYLAVV ESLAKLVATG
FTRDAAYLSF QEYFGRLGDD PIRWGRPTAS VLGALMAQVD LGVAAIGGKD SMSGTFEGLD
VPPTLISFAV SVGDASHVVS PEFKGAGHRI VRIAPKYGDE RAVGGSQGKV DQHCAVYGAY
DLIPRSKSLL SVMDVVQALA ADGSALAIST PGYGAAAEAL FKMALGNRIG LRLAGIDVDD
LFVPAYGSFL IELKDGAGLP DVDPDSMDMQ VIGETTADYR FTVVSPKAQS WRGCRQASMS
DDDGRVCGSH ADGFHAEPDD EDMMCESADL DDVQERWEGV LESVYPYRSK ACAAASAAAN
RDRYGTSAVP TLNFDVPAFR SSRPRHVGGV RPRVVIPVFP GNNCEYDSAQ AFRRAGAEVH
TLIINNLTAG AVAGSAKALA AAIRASQIVM IPGGFSGGDE PDGSAKFIAA FFRSPEVADA
VRDLLHNRDG LMLGICNGFQ ALVKLGLLPY GDIVDMTSQC PTVTFNTIGR HQSRLVRTRV
ASTKSPWLSL TSVGAVHTVA VSHGEGRFVA SPHLLRQLVD DGQIATQYVG DDGRPSMDLS
VNPNGSVFAV EGVTSPDGRI LGKMGHSERS GDNLYRNVPG DHYQPVFEAG VAYFA
//
