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Database: UniProt
Entry: R5E692_9FIRM
LinkDB: R5E692_9FIRM
Original site: R5E692_9FIRM 
ID   R5E692_9FIRM            Unreviewed;      1250 AA.
AC   R5E692;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:CCX83651.1};
GN   ORFNames=BN798_02143 {ECO:0000313|EMBL:CCX83651.1};
OS   Eubacterium sp. CAG:86.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262895 {ECO:0000313|EMBL:CCX83651.1, ECO:0000313|Proteomes:UP000017940};
RN   [1] {ECO:0000313|EMBL:CCX83651.1, ECO:0000313|Proteomes:UP000017940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:86 {ECO:0000313|Proteomes:UP000017940};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCX83651.1}.
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DR   EMBL; CAXC010000116; CCX83651.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5E692; -.
DR   Proteomes; UP000017940; 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; 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.
PE   4: Predicted;
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:UP000017940}.
FT   DOMAIN          180..229
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"
SQ   SEQUENCE   1250 AA;  138384 MW;  667F674EA79B231F CRC64;
     MSGVKRVFVE KKKPYAVKAK ELYDEITDYL GIKTVTGVRV LIRYDIENLS DDTYKKALTT
     VFSEPPVDDV YEMQFESGND DYVFSVEYLP GQFDQRADSA EQCVKFFNEN EIPVIKTATT
     YVISGTLTDE QKEKIKELCI NPVDSREADS KIPDTLVTEF KVPADVIIFD GFKDMAEADL
     KELYDSLGLA MTFKDFIFIQ EYFKNEEKRD PSMTEIRVLD TYWSDHCRHT TFATELKDVK
     FKDGFYRKPM EDTYKKYLSD RAEIYKGRKD KFVCLMDLAL MAMKKLKAEG KLNDQEESDE
     INACSIVVPV TIDGKEEEWL VNFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRTYVYQ
     AMRVTGAADP TKPMSETLHG KLPQKKLVTG AAHGYSSYGN QIGLATGYVK EIYHHDYVAK
     RMEIGAVIAA APRSAVKREN SDPGDIIILL GGRTGRDGCG GATGSSKVHT EKSIETCGAE
     VQKGNAPTER KMQRLFRRPE VTKLIKKCND FGAGGVSVAI GELAAGLRVS LDKVPKKYEG
     LDGTELAISE SQERMAVVID PKDVRAFLNY AAEENLEAVE VATVTEEPRL VLEWRGKEIV
     NISRAFLDTN GAHQETSVLV DIPSKEDSYL KSSKIEDVRG KWLKVLSDLN ECSQKGLVER
     FDGSIGAGSV YMPFGGKYQL TETQAMVAKL PVLKGKCDTV TMMSYGFDPY LSKWSPYHGA
     IYAVTDSVAK IVAAGGDFNK IRFTFQEYFR RMTEDPSRWS QPFAALLGAY EAQLGFGLPS
     IGGKDSMSGT FEEIDVPPTL CSFAIDVAKE GDIITPELKT PGNVLVKFDI EHDEYDIPVF
     EQVKALYNSI HELTENGTIV SAYVCDANGF VPALCKMAFG NKLGFALNSD LKEESLFAPA
     YGCIVAEVAK DKLDKIKTAY TKLGEVKEKA AFTYKEVSIN VEEALSVWED KLEKVFPTKV
     SKETTSIETK LFNAENVHVC KNKVAKPTVF IPVFPGTNCE YDSTKAFERA GADVIVKVFK
     NLDAAGIRES VDEFEKAIAQ SQIIMFPGGF SAGDEPDGSA KFFATAFRNA KMKEAVEKLL
     NERDGLALGI CNGFQALIKL GLVPNGAITG QNEQSPTLTF NTINRHISKM VYTKVVSNLS
     PWLAGAELGG VYCNPASHGE GRFVAPKEWL DKLFANGQVA TQYCDINGNI SMDEEWNVNG
     SYMAIEGITS PDGRCLGKMA HSERRGDGVA INIYGEQDLR IFESGVAYFK
//
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