ID A0A239ZR97_CLOCO Unreviewed; 1257 AA.
AC A0A239ZR97;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:SDK81177.1, ECO:0000313|EMBL:STA92196.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:STA92196.1};
GN Name=purL {ECO:0000313|EMBL:STA92196.1};
GN ORFNames=NCTC2909_00870 {ECO:0000313|EMBL:STA92196.1},
GN SAMN05216497_10158 {ECO:0000313|EMBL:SDK81177.1};
OS Clostridium cochlearium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1494 {ECO:0000313|EMBL:STA92196.1, ECO:0000313|Proteomes:UP000253892};
RN [1] {ECO:0000313|EMBL:SDK81177.1, ECO:0000313|Proteomes:UP000198811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-C224 {ECO:0000313|EMBL:SDK81177.1,
RC ECO:0000313|Proteomes:UP000198811};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:STA92196.1, ECO:0000313|Proteomes:UP000253892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC2909 {ECO:0000313|EMBL:STA92196.1,
RC ECO:0000313|Proteomes:UP000253892};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNGL01000001; SDK81177.1; -; Genomic_DNA.
DR EMBL; UFWH01000001; STA92196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239ZR97; -.
DR STRING; 1494.SAMN05216497_10158; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000198811; Unassembled WGS sequence.
DR Proteomes; UP000253892; 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; 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; 2.
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:STA92196.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 181..229
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 442..594
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1098
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1257 AA; 140527 MW; 5B4F352B63D39CA4 CRC64;
MKKNIFRLYV EKKDKFDVES INLKQDLKLT LGIEEISKLK IVNIYDIEGL DIEELKKAKN
TVFSDPVVDN VYEEEFPIGK GAKFFVSEYL PGQYDQRADS SVQCVQILTG KSGIDIKTSK
LFIVEGIQKD EDFKKIKDYC INDVDSREGS INKPNTLDLN FVEPKNVKTL EGFIDLKEDE
LEELLKHEGL AMDIEDLKYC QAYFKKEHRN PTITEIKVID TYWSDHCRHT TFNTEIKNVK
IEETDLTKPI KEVYEDYLNS REFIHKDRDD KYQSLMDIAT IGMKEALKRG MLQRLDKSEE
INACSIKVEA DVNGKPEEWL IMFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRAYVYQ
AMRVTGSADP RRKIEDTIKG KLPQKKITTE AAAGYSSYGN QIGVSTGFVD ELYHEGYMAK
RMEVGAVIGG VKASNVVRES PRKGDVVILL GGKTGRDGCG GATGSSKEHT EESIVECSSE
VQKGNAPTER KIQRLFRNEE VCKMIKRCND FGAGGVSVAV GELTDGLYID LDKVPKKYEG
LDGTEIAISE SQERMAIVID GKNLERFISL AEEENLEATK IADVTSNKTL EMYWRGDKIV
DLKREFLDSN GVKKEIDVEV SSPKKEENYF TKCSNKYKNI KEAWLETLSN LNVCSKKGMV
ERFDNTVGAS TVLMPFGGKY ALTPSEGMVA KIPVLHGETT TATIMSHGFN PYISEWSPFH
GALYAVLESI AKIVALGGDY KDIHLSFQEY FESLGEDKTK WGKPFAALLG ALKAQKEFKA
FAIGGKDSMS GTFKELDVPP TLISFALGLL NTNNSISQEF KEINSNVVIL KVDRDENYIP
NLDMAKKNFE VVHSLIKSGK ALSTYTIKAG GIIEAISKMA FGNKIGISFD NNKEWTVEEL
LDPSYGSIIV ELNKDINLEE ELKGSNWELL GKTIEEQCFK VKDEVIKIDE ALESWIKPLE
TVFPTKIEDI KEDINNINFQ KDNKNISIIK NIKPQVFIPA FPGTNSEYDT AKAFIKAGGQ
VSSLVFRNNS IKDIEETIDA YAKEIRNSNI LAIPGGFSAG DEPDGSGKFI ATVFRNEKIK
DAVMDLIKNR DGLILGICNG FQALIKLGLI PYGEIRELDE KSPTLAQNKI GRHVSKIVRT
KVVSNLSPWF NNVKVGDVFS LPISHGEGRF MADEDVLRKL IDNGQIASQY VDLNGNATYD
IEFNPNGSLY AVEALTSPDG RILGKMAHSE RIGEGLYRNI PGEKDQKIFE AGINYFK
//
