ID A0A151AM52_9CLOT Unreviewed; 1254 AA.
AC A0A151AM52;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:KYH28610.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:KYH28610.1};
GN Name=purL {ECO:0000313|EMBL:KYH28610.1};
GN ORFNames=CLCOL_18710 {ECO:0000313|EMBL:KYH28610.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH28610.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH28610.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH28610.1,
RC ECO:0000313|Proteomes:UP000075374};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium colicanis DSM 13634.";
RL Submitted (FEB-2016) 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:KYH28610.1}.
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DR EMBL; LTBB01000009; KYH28610.1; -; Genomic_DNA.
DR RefSeq; WP_061858697.1; NZ_LTBB01000009.1.
DR AlphaFoldDB; A0A151AM52; -.
DR STRING; 1121305.CLCOL_18710; -.
DR PATRIC; fig|1121305.3.peg.1873; -.
DR Proteomes; UP000075374; 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:KYH28610.1};
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:UP000075374}.
FT DOMAIN 181..230
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 445..595
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1095
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1254 AA; 140247 MW; FAC1F0713B916587 CRC64;
MKTEIKRIFV EKKSPFDVEA KGLLKDIREN LNIKTIENLR ILNRYDVSGI SKEEYEKAKH
IIFSEPVVDM VYDEKITVKK GEKIFAVEYL PGQYDQRADS AAQCIQILTQ NKKPIVRCAK
VIIISGDVSS EELESIKKYY INTVDSMETT LEKPLSLEMN LKAPEDVEIL EDFIDKDSDE
LKEFMNDNGL AMSFEDLKFC QDYFKNIEKR NPTITEIKVI DTYWSDHCRH TTFQTQIQEV
EFQEGKYTDI IKKTYEEYKN LRNYVYEDKE KNKDICLMDI ATIGMKELRK KGLLEDLEVS
DEINACSIEC DVDVDGKSEK YLVMFKNETH NHPTEIEPFG GAATCLGGAI RDPLSGRSYV
YGAMRVTGSA DPRKPVEETL KGKLPQRQIT IKAAQGYSSY GNQIGLATGH VAEVYDEGFL
AKRMEIGAVI GAAPKENVIR ETPIEGDSII LVGGRTGRDG CGGATGSSKE HDETSILNCG
AEVQKGNAPE ERKLQRLFRN PKVSRIIKRC NDFGAGGVSV AIGELSEGLS INLDLITKKY
EGLNGTELAI SESQERMAVV VGKDDAAKFI EYAKEENLEA VEVAKVSGDR RLKMLWRGQT
IVDISRDFLD TNGVKQKINV KVQSPSEKSY FKVTNIEDIK GKWIETIENL NICSQKGLVE
RFDNTIGSST VLMPFGGKYC KTPAEAMCFK IPVLNGESST CTLMSYGYNP KIGKWSPFHG
ALYAIVEAVT KIVASGGDYK NVRLTLQEYF EKLGDDPKKW GKPLSALLGA LYAQRKLGIA
AIGGKDSMSG TFKDISVPPT LVAFAVNVTN IDNIISPEFK KKGSKVILIK TPKNENDIPD
FNELKKNYEL VNRLINRKLV LSAYSVKMGG IAEAISKMSF GNKIGFNFSN NIKVEDLFTP
DYGSIILEIC NKVELKKELN DINYILLGFT QSTRKIKIKD VEIDLETLIE HWERPLENVF
PTKVEKICED IELQLYEGKI SRGPCIKLPK PKVYIPVFPG TNCEYDIEKR FKAAGAETKV
SVFRNLTSKD IKESIEDMVD SINNSQIIAL PGGFSAGDEP DGSGKFIATV FRNPKVKDAV
MKFLNYRDGL ILGICNGFQA LIKLGLLPYG EIRNIDEESP TLTYNTIGRH SSKFVMTKKV
SNLSPWLSNI SLGDVYSIPI SHGEGRFVCT PKMAQELLKN GQIATQYVDF CGNPTYDIEF
NPNGSMYAVE GITSPDGRIF GKMGHSERIG ENLYKNIAGE KDQKIFEAGV SYFK
//
