ID D8IDB1_BRAP9 Unreviewed; 1248 AA.
AC D8IDB1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:ADK31134.1};
GN Name=purL {ECO:0000313|EMBL:ADK31134.1};
GN OrderedLocusNames=BP951000_1144 {ECO:0000313|EMBL:ADK31134.1};
OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK31134.1, ECO:0000313|Proteomes:UP000000332};
RN [1] {ECO:0000313|EMBL:ADK31134.1, ECO:0000313|Proteomes:UP000000332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT "The complete genome sequence of the pathogenic intestinal spirochete
RT Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL PLoS ONE 5:E11455-E11455(2010).
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DR EMBL; CP002025; ADK31134.1; -; Genomic_DNA.
DR RefSeq; WP_013244087.1; NC_014330.1.
DR AlphaFoldDB; D8IDB1; -.
DR STRING; 759914.BP951000_1144; -.
DR GeneID; 56439709; -.
DR KEGG; bpo:BP951000_1144; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_003100_2_0_12; -.
DR InParanoid; D8IDB1; -.
DR Proteomes; UP000000332; 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; 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 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:UP000000332}.
FT DOMAIN 173..222
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 444..596
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1089
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1248 AA; 140555 MW; 392FFD405C3601C8 CRC64;
MNYRIFIEKK EGFDLEAKRL ESQLKENFKI KCNVRLLNVY DIFNIEESKL KNSINVIFSE
PPTDRVVEKK DFESLKHFAV EYLPGQFDQR ADSALQCLKL IYNDIEEVTI VSGKVILFDG
NVDDITIEKI KKFYINPVES REKDLRKLEI EPHQKADDIK DVKNFINLNT EELHKYRDNL
DLAMTYKDIE FVQNYFKNEE KRNPTETEIK VLDTYWSDHC RHTTFMTKIN DVKLENDKSN
FSEVILNAIN KYYSMRKELY GEDVDSKRDI NLMDMATVSA KYIKKKGKLE DLEISDEINA
CSIYIDVDAV DDNGKNKTEK YLLMFKNETH NHPTEIEPFG GASTCLGGAI RDPLSGRSYV
YQAIRVTGSA NPLEKLEDTL PGKLPQKKIT TTAAAGYSSY GNQIGLTTCL VNEIYDEGYK
AKRLEVGAVV GAVPVDYVRR EKPKAGDIVI VLGGRTGRDG CGGATGSSKS HTDTSLRLCG
AEVQKGNAPE ERKIQRLFRN KEVTKLIKKC NDFGAGGVSV AIGELSDGID INLDVLPVKY
LGLNGTELAI SESQERMAVV VESKDADNFI KLANKENIEA TKVATITDTN RLVMYLKGKK
IVDISRKFLD TNGAKQETNA VLKNIDFENN PFNTKNACSL TSHWFNMAEN LNVASQKGLI
EMFDSSIGAT TVLMPFGGKY QMTPSDVSIQ KIPIFDNNAK QINTASAISW GYNPSIMKWS
EFHGGIYSVI ESMSKLVSIG ADYKNIRLSF QEYFEKLGND PKKWGKVYSA LLGTIYAQTE
FDIPAIGGKD SMSGTFNNIS VPSTLISFAV STVNSNDVIS PEFKSSNNYV YLIKHNMLEN
YMPNVAEIKE NFEFIHKNIK DKKILSAYTI KFGGIAEALT KMSFGNRIGV DIKDELYFFN
LMPASFIVET KEELNYKNAL LIGKTINEYK IKVCGEIVDL EELEKLWLDK LSTVFPYKTY
EDIETYQLAE YKREAPFICK NKTAKPNVLI SAFLGTNCEY DTQKAFSDAG ANTDIFVFRN
IKPEYIKESI EEMSKKIDNS QIFMIPGGFS AADEPDGSGK FISAILTNEK IKTSIHKLLE
RDGLVLGICN GFQALIKSGL LPYGKIGNIT EKSPTLTFNK IGRHISQMVT TKVVSNNSPW
LYNIPLGSEL VVPVSHGEGR FFADEDIIKE LIKKGQIATQ YVNFESKPTN EFRFNPNGSA
YAIEGILSED GKVFGKMGHS ERYGNNLYKN IITKDIYNIF ENGVNYFK
//
