ID A0A0F2E6K4_STROR Unreviewed; 1241 AA.
AC A0A0F2E6K4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:KJQ78034.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:KJQ78034.1};
GN Name=purL {ECO:0000313|EMBL:KJQ78034.1};
GN ORFNames=TZ95_00232 {ECO:0000313|EMBL:KJQ78034.1};
OS Streptococcus oralis subsp. tigurinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1077464 {ECO:0000313|EMBL:KJQ78034.1, ECO:0000313|Proteomes:UP000033377};
RN [1] {ECO:0000313|EMBL:KJQ78034.1, ECO:0000313|Proteomes:UP000033377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC5873 {ECO:0000313|EMBL:KJQ78034.1,
RC ECO:0000313|Proteomes:UP000033377};
RA Haase E.M.;
RT "Evolution of amylase-binding proteins of oral streptococcal species.";
RL Submitted (FEB-2015) 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:KJQ78034.1}.
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DR EMBL; JYGU01000004; KJQ78034.1; -; Genomic_DNA.
DR RefSeq; WP_045616621.1; NZ_JYGU01000004.1.
DR AlphaFoldDB; A0A0F2E6K4; -.
DR PATRIC; fig|28037.217.peg.213; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000033377; 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: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; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:KJQ78034.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 182..228
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 439..591
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 1241 AA; 135574 MW; A4BC47BBD303F9EA CRC64;
MNKRIFVEKK ADFQVKSESL VRELQHNLGL STLKSIRIVQ VYDVFDLAED LFAPAEKHIF
SEQVTDYVLD KATVQADLAN YAFFAIESLP GQFDQRAASS QEALLLLGSS SDVTVNTAQL
YLVNKDIDAT ELEAVKNYLL NPVDSRFKDI TTGIAKQEFS ESDKTIPKLN FFESYTAEDF
ARYKAEQGMA MEVDDLLFIQ DYFKSIGRVP TETELKVLDT YWSDHCRHTT FETELKNIDF
SASKFQKQLQ VTYDKYIAMR DELGRSEKPQ TLMDMATIFG RYERANGRLD DMEVSDEINA
CSVEIEVDVN GVKEPWLLMF KNETHNHPTE IEPFGGAATC IGGAIRDPLS GRSYVYQAMR
ISGAGDITTP ISETRDGKLP QQVISKTAAH GYSSYGNQIG LATTYVREYF HPGFVAKRME
LGAVVGAAPK GNVVREKPEA GDVIILLGGK TGRDGVGGAT GSSKVQTVES VETAGAEVQK
GNAIEERKIQ RLFRNGDVTR LIKKSNDFGA GGVCVAIGEL ADGLEIDLNK VPLKYQGLNG
TEIAISESQE RMAVVVRPGD VDAFVAECNK ENIDAVVVAT VTEKPNLVMH WNGETIVDLE
RRFLDTNGVR VVVDAKVVDK DVKLPEERQT SAENLEADTL EVLDDLNHAS QKGLQTIFDC
SVGRSTVNHP LGGRYQITPT EASVQKLPVQ HGVTTTASVM AQGFNPYVAE WSPYHGAAYA
VIEATARLVA TGANWSKARF SYQEYFERMD KQAERFGQPV AALLGSIEAQ IQLGLPSIGG
KDSMSGTFEE LTVPPTLVAF GVTTADSRKV LSPEFKTAGE NIYYIPGQAL SAEIDFDLIK
KNFAQFEAIQ ADHKVPSASA VKYGGVLESL ALATFGNHIG AEVTLPELET ALTAQLGGFV
FTSPEEIAGV EKIGQTKADF TLLVNGVKLD GQKLDSVFQG KLEEVYPTEF TQAKELAEVP
AVASNANIKA KETIEKPVVY IPVFPGTNSE YDSAKAFEKE GAEVNLVPFV TLNEEAIVKS
VETMVDNIGK ANILFFAGGF SAADEPDGSA KFIVNILLNE KVRVAIDSFI ARGGLIIGIC
NGFQALVKSG LLPYGNFEDA TSTSPTLFYN DANQHMAKMV ETRIANTNSP WLAGVQVGDI
HAIPVSHGEG KFVVTAEEFA ELRDNGQIFS QYVDFDGKPS MDSKYNPNGS VNAIEGITSK
NGQIIGKMGH SERYEDGLFQ NIPGNKDQHL FASAVRYFTG K
//
