ID A0A0P8WDR9_9CLOT Unreviewed; 1260 AA.
AC A0A0P8WDR9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase 2 {ECO:0000313|EMBL:KPU45887.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:KPU45887.1};
GN Name=purL {ECO:0000313|EMBL:KPU45887.1};
GN ORFNames=OXPF_03550 {ECO:0000313|EMBL:KPU45887.1};
OS Oxobacter pfennigii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU45887.1, ECO:0000313|Proteomes:UP000050326};
RN [1] {ECO:0000313|EMBL:KPU45887.1, ECO:0000313|Proteomes:UP000050326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU45887.1,
RC ECO:0000313|Proteomes:UP000050326};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL Submitted (SEP-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:KPU45887.1}.
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DR EMBL; LKET01000016; KPU45887.1; -; Genomic_DNA.
DR RefSeq; WP_054873506.1; NZ_LKET01000016.1.
DR AlphaFoldDB; A0A0P8WDR9; -.
DR STRING; 36849.OXPF_03550; -.
DR PATRIC; fig|36849.3.peg.385; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000050326; 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:KPU45887.1};
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:UP000050326}.
FT DOMAIN 188..230
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 443..594
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1100
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1260 AA; 139633 MW; 8CA5B62E64CD2740 CRC64;
MRDKVRRIFV EKKKGFDVEA KNLTDDIKEN LIIAGLHNIR IINRYDISGM TDDEYEKSKY
IIFSEPPVDD VYDEALNLKG GLRAFAIEYL PGQYDQRADS AAQCVQILTQ KERPEVLSAK
VIVIEGDISD SDFGRIKSYC INPIESREAS LEKPETLEVN YNEPEDVEVL KGFTGFSKEK
LDEFMTFMGL AMSMEDLIFV QEYFKDTEKR DPSITEIRVI DTYWSDHCRH TTFLTNIKEV
SIEEGKYKSV IEKVLSDYMA SRKYVYGDRE KDVSLMDLAT ISMKELRKKG YLKDLDESEE
INACSIAVNV DVDGRDEEWL IMFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRSYVYQ
AMRVTGSGDP RTKIEDTLSG KLPQRKITTG AAAGYSSYGN QIGLSTGLVS EVYHPDFVAK
RMEIGAVIGA APKGNVVRLS PTPGDKIILL GGRTGRDGCG GATGSSKEHD EESLLSCGAE
VQKGNPPTER KIQRLFRNPE VSKLIKRCND FGAGGVSVAI GELADGLEID LDKVPKKYEG
LDGTELAISE SQERMAVVVS QADVERFIAL AGGENLEAVE VAQVTDKNRL KMTWRGKEIV
DISRDFLNTN GAKQYSNAHI KLPKEENNYF KARLENFDSK QKSLKEKWLD NLRDLNVCSQ
KGMVERFDST IGAGTVLMPF GGKFQLTPME VMAARIPVLK GETRTGTLMS YGYNPELAKW
SPFHGAVYAI TEAVTKIVAA GGNYKNIRLT LQEYFEKLGK DPEKWGKPLG ALLGSYYTQM
KLSIPAIGGK DSMSGTFKDL NVPPTLVAFA VNLINTDEVI SGEFKGKGSQ VVLIPCPRDE
YNLPVFEVLE FNFEKITELI NKGKVLSSYT VRLGGIAEAV SKMSFGNSIG FDFAEDMEEE
KLFSSDYGSI ILEIPKEEKL DEILRDVEYK LLGHTTEDKC IKAKYMALDL DEAVNAWMEP
LEKVFPTKAK ALDTKLETFE SNIKSSLKPR VSSMKPRIFI PVFPGTNCEY DTARAFEKAG
GTADIFVVKN LTPKDIEETL NELCKRIESS QIIAIPGGFS GGDEPDGSGK FIATALRNPK
VKDAVMNLLK NRDGLMIGIC NGFQALIKLG LVPYGEVRDI DSTSPTLTFN TLGRHISRMV
QTKIASTASP WFNNVKAGDV HTVAVSHGEG RFWATEDVVD SLVKNGQIAT QYVDFSGKPT
MDISYNPNGS ICAIEGITSP DGRILGKMGH SERAGYNVFT NIPGDKDQKI FKAGVDYFKI
//
