ID K2LBZ4_BIFBI Unreviewed; 832 AA.
AC K2LBZ4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:EKF15409.1};
DE Flags: Fragment;
GN ORFNames=B217_07244 {ECO:0000313|EMBL:EKF15409.1};
OS Bifidobacterium bifidum IPLA 20015.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1207543 {ECO:0000313|EMBL:EKF15409.1, ECO:0000313|Proteomes:UP000007366};
RN [1] {ECO:0000313|EMBL:EKF15409.1, ECO:0000313|Proteomes:UP000007366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPLA 20015 {ECO:0000313|EMBL:EKF15409.1,
RC ECO:0000313|Proteomes:UP000007366};
RA Gueimonde M., Margolles A., Sanchez B.;
RT "Genome sequence of Bifidobacterium bifidum IPLA 20015.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EKF15409.1}.
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DR EMBL; AMPM01000233; EKF15409.1; -; Genomic_DNA.
DR RefSeq; WP_003821824.1; NZ_AMPM01000233.1.
DR AlphaFoldDB; K2LBZ4; -.
DR PATRIC; fig|1207543.3.peg.1315; -.
DR Proteomes; UP000007366; Unassembled WGS sequence.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 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; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010141; FGAM_synthase.
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; 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; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT DOMAIN 17..168
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 672
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 804
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKF15409.1"
SQ SEQUENCE 832 AA; 88580 MW; 75221508B674E2AE CRC64;
VVAATPADHV RRETPAPGDR IILLGGRTGR DGIGGATGSS KAHNVESLEL DGAEVQKGNA
PVERKLQRLF RRGDACRLIK RCNDFGAGGV SVAVGELADG LYVDLNTVPK KYEGLDGTEL
AISESQERMA VDVAAEDVDE FLGYAREENL EATVIATVTE DPRMVMTWNG DKIVNLSREF
LASNGASKHQ VVRVEEQEAY EVPASWREGS LADRMNAVVT DLNVASNKGL SERFDSTIGA
GTVLMPFGGR KQLTPNEAMV AKLPVFGETT TASAMAWGFN PYIMSKNQFT GAYLSVVESL
SKLVAAGFEH EKAYLSFQEY FEKLRDEPER WGKPTAAVLG ALMAQVDLGA GAIGGKDSMS
GSFENLDVPP TLISFAVAVG SMKRATSPEF KGAGHRIVRI APRYLADGLT PDKNALLEAF
SLVEELTDPS HHIALAVSTP GYGATAEALF KMTLGNRIGL TLNESIAADD LFKPAYGSFI
IELADNEKIP VASNLVEVGE IGTTTAEYVF KAAGETLDLA NVQEAWESGI ESVFPYRSKS
DEAGKSVETI TFDAPKKTVY TGAGIAKPHV VIPVFPGNNC EYDSAAAFER AGADVTTLIV
NNLTPAAVAE STQALVDEIN KSQIVMIPGG FSGGDEPDGS AKFITAFFRA PAVTEAVRDL
LKNRDGLMLG ICNGFQALIK LGLVPYGDIV PMTAECPTLT FNTIGRHQSR LVRTRVASNL
SPWLSRTAVG DVHTVAISHG EGRFVAAEPV LDLLKANGQI ATQYVDEAGV PGMDLTVNPN
GSLLAIEGIT SPDGRVFGKM GHSERSGNGL YVNVPGDKYQ PIFEAGVGYF AA
//