ID   R6QUE9_9FIRM            Unreviewed;      1250 AA.
AC   R6QUE9;
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:CDC36609.1};
GN   ORFNames=BN606_00651 {ECO:0000313|EMBL:CDC36609.1};
OS   Butyrivibrio sp. CAG:318.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio; environmental samples.
OX   NCBI_TaxID=1262761 {ECO:0000313|EMBL:CDC36609.1, ECO:0000313|Proteomes:UP000018075};
RN   [1] {ECO:0000313|EMBL:CDC36609.1, ECO:0000313|Proteomes:UP000018075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:318 {ECO:0000313|Proteomes:UP000018075};
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:CDC36609.1}.
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DR   EMBL; CBFF010000024; CDC36609.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6QUE9; -.
DR   STRING; 1262761.BN606_00651; -.
DR   Proteomes; UP000018075; 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:UP000018075}.
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;  138066 MW;  94073ECE1A0A0B6F CRC64;
     MSNVKRVYSE KKPEFAVKAK ELSEEISSYL NIDTVTNVRV LIRYDIEGIT EDTYRKALVT
     VFSEPPVDIV YEEDFEHRPG EHVFAVEFLP GQFDQRADSA VQCVKLLRED EDVEIKTATV
     YAVEGSLTDS QLESIKNFCI NPVDSREAKM DKPETLVTIF PDPADVKIFD GFKDMPETEL
     KELYSSLGLA MTFKDFLHIQ KYYHDEEHRD PSMTEIRVLD TYWSDHCRHT TFSTELKNIR
     FGEGYYRKPI EDSFDKYKET FGELYAGRDD KFVCLMDIAL MAMKKLKKDG KLQDMEVSDE
     INACSIVVPV TIDGVTEEWL VNFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRTYVYQ
     AMRVTGAADP TVSLDKTMAG KLPQKKIVRE AAHGYSSYGN QIGLATGYVK EIYHPNYAAK
     RMEIGAVMGA APRSAVIRET SDPGDIIILL GGRTGRDGCG GATGSSKAHT EKSIDTCGAE
     VQKGNAPTER KIQRLFRRPE VSSLIKKCND FGAGGVSVAI GELADGLRVS LDKVPKKYAG
     LDGTELAISE SQERMAVVVD PKDVKAFLEY ANEENLEAVE VAVVTEEKRL ILEWRGKEIV
     NISRAFLDTN GAHQETDVVV NIPEEKDNLF KAPEVKDVKA EWLKTLSDLN VCSQKGLVEM
     FDGSIGAGSV FMPYGGKYQL TEVQTMVAKL PVLKGKTDFV TMMSYGFDPY LSSWSAYHGA
     IYAVVESMAK IVCAGGDFKK IRFTFQEYFR RMTEDPARWG EPMKALLGAF DAQMGFGLPS
     IGGKDSMSGT FNDLDVPNTL VSFAVDTGSY NDIITPEFKK AGNKIVLFEI ERDEYDLPVY
     SQVMALYNAV AKAIADKAVV SAYTLNAKGI AEAVSKMAFG NKLGVRINAD YDSSEFFAPK
     YGCIIAEANP ELLDKIGCKY TVIGEVTDDG TFTYGDAVIS VEEALNTWKK PLEKVFPTVA
     VKGGQKLETP VYNADSIYVC KNKVAKPTVF IPVFPGTNCE YDSTKAFENA GANVVTKVFK
     NLTAADIRDS VDEFEKAINQ AQIIMFPGGF SAGDEPDGSA KFFATAFRNA KIKEAVDKLL
     NERDGLALGI CNGFQALIKL GLVPYGRITE QKADSPTLTM NTIGRHISKM VYTKVVSNKS
     PWLAGAKLGG VYVTPASHGE GRFVADKEWL DRLFAEGMVA TQYVDIDGNP TMDEEWNVNG
     SYRAIEGITS PDGRVFGKMA HVERKGDAVA VNIFGEQDLK VFESGVKYFK
//