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Database: UniProt
Entry: R7JUP2_9FIRM
LinkDB: R7JUP2_9FIRM
Original site: R7JUP2_9FIRM 
ID   R7JUP2_9FIRM            Unreviewed;      1265 AA.
AC   R7JUP2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:CDE67361.1};
GN   ORFNames=BN630_02214 {ECO:0000313|EMBL:CDE67361.1};
OS   Blautia sp. CAG:37.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1262757 {ECO:0000313|EMBL:CDE67361.1, ECO:0000313|Proteomes:UP000018204};
RN   [1] {ECO:0000313|EMBL:CDE67361.1, ECO:0000313|Proteomes:UP000018204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:37 {ECO:0000313|Proteomes:UP000018204};
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:CDE67361.1}.
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DR   EMBL; CBJJ010000259; CDE67361.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7JUP2; -.
DR   Proteomes; UP000018204; 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:UP000018204}.
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   1265 AA;  139794 MW;  BF12F2A4C729AB86 CRC64;
     MSTVRRVYVE KKPEFAIKAK DLKHEIKHYL NIQTVTNVRE LIRYDVENIS DETYEKACKV
     VFAEPPVDIC YQEDFPRAEG ARVFSVEFLP GQFDQRADSA VQCVQFLKED EQPIIRSAVT
     YVIEGEMTDE QFDAVKAHCI NPVDSRETGL EKPETLVTKF EEPADVKIFD GFIDMPEAEL
     KALYDSLGLA MTFKDFLHIQ NYFRGEEKRN PSMTEIRVLD TYWSDHCRHT TFSTELTNVT
     FGEGDYYEPM KKSYDRYLSD REVLYKGRDD KFICLMDLAL LAMKKLKSEG KLADQEESDE
     INACSIVVPV DVDGKDEEWL INFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRTYVYQ
     AMRVTGAADP TRPQSETLEG KLPQKKLVRE AAHGYSSYGN QIGLATGYVK EVYHPDYVAK
     RMEIGAVLGA APRRAVVREN SDPGDIIILL GGRTGRDGCG GATGSSKVHT TESIETCGAE
     VQKGNAPTER KLQRLFRREE VSLLIKKCND FGAGGVSVAI GELAPGLKIN LDKVPKKYAG
     LDGTEIAISE SQERMAVVID PKDREQFLKY AAEENLEATE VAVVTEDPRL VLSWRGKEIV
     NISRAFLDTN GAHQENDVFV EIPKAEDTPL KRSGDIADVK EKWLSTLSDL NACSQKGLVE
     MFDSSIGAAS VLMPYGGKYQ LTETQAMVAK VPVPDGKTNT VTMMSYGFDP YVSSWSPYHG
     AVYAVTESLS RIVAVGGDYS KVRFTFQEYF RRMTEDPHRW SQPFAALLGA YDAQMGYGLP
     SIGGKDSMSG TFNHIDVPPT LVSFAVDVAK LKDVVSPELK NTGDKLVWIH LPVDAHLLPE
     YEGVMETYRK LHEDMQNGRV KAAYVVDRQG IAAAVSKMAF GNALGVTIEH NVDERDLFTP
     YIADLICEVP AEKVGELAST YTVIGEVTDK PVLSYKDTEI TIREAVSAWN KPLEKVFKTV
     SGAELPEVDA LNVAAADENG IVADSCYQAK SIHVCSHKLA QPTVFIPVFP GTNCEYDSTR
     AFERAGAKVI TQVFSNLSAE DIRGSVDAFE KAINQAQIIM FPGGFSAGDE PDGSAKFFAT
     AFQNAKIKEA VTKLLNERDG LALGICNGFQ ALIKLGLVPY GEILGQTEDS PTLTFNTIGR
     HISKMVYTKV VTNKSPWLAG AELGGVYTNP ASHGEGRFVA SKEWIDKLMA NGQIATRYCD
     VNGNLTNDEY WNVNGSYCGI EGITSPDGRV FGKMAHAERR DNGVAVNIYG EQDLKIFESG
     VAYFK
//
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