ID R6MT39_9FIRM Unreviewed; 1255 AA.
AC R6MT39;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:CDC02888.1};
GN ORFNames=BN531_00368 {ECO:0000313|EMBL:CDC02888.1};
OS Eubacterium sp. CAG:202.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262884 {ECO:0000313|EMBL:CDC02888.1, ECO:0000313|Proteomes:UP000017996};
RN [1] {ECO:0000313|EMBL:CDC02888.1, ECO:0000313|Proteomes:UP000017996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:202 {ECO:0000313|Proteomes:UP000017996};
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:CDC02888.1}.
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DR EMBL; CBEO010000144; CDC02888.1; -; Genomic_DNA.
DR AlphaFoldDB; R6MT39; -.
DR STRING; 1262884.BN531_00368; -.
DR Proteomes; UP000017996; 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; 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; IPR016188; PurM-like_N.
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; PF00586; AIRS; 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 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:UP000017996}.
FT DOMAIN 181..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"
FT DOMAIN 715..797
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT ACT_SITE 1096
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1255 AA; 136725 MW; E9BF3E66258FB468 CRC64;
MSGVIRIFVE KRDGFNVLAK QTLWDIRHNL GMRNVTDLRY IMRYDIEGLS LDEYNAAKGT
ILSEPNADVI YEETLPVEDG WKVFAMEYLP GQYDQRGDSA EQCVQLLTQG ERCKVLTARV
VAVTGDISDD DLKKIEDYLI NPVESRLASL EKPQTLDIAT PVPADVKRVE GFIKFNDEEM
EKYYGSMGFA MTLSDLKFCR DYFRDTEKRD PSVTELRVID TYWSDHCRHT TFLTKLEKIE
VEKAALGSVI EDALNEYYAT RDEVYGKDTK RIVSLMDMAL IGMKSLKKKG LIPDLDESEE
INACSIEVPV TIDGKTEQWL VQFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRSYVYQ
AMRVTGSGDP TIPVKDTMPG KLPSRKITTG AANGYSSYGN QIGLATGQVT ELYDSGYVAK
RLEIGAVIGA SPKENVIREV PLPDDIIVLL GGRTGRDGCG GATGSSKAHT ESSIETCGAE
VQKGNPPTER KIQRLFRNPK VAKLIKRCND FGAGGVCVAI GELADGLAVD LDKVTKKYDG
LDGTELAISE SQERMAVVLD KKDVETFIAE AEKENLEATA VAVVTESPRL TMTWRGDKIV
DLSREFLNTN GVTQLSSAYI TAPKAEDCYR KACPDVLKDM PADKALEENM ARLEVCSQIG
LSERFDASIG AATVIMPFGG KNQLTPQEAM AAKIPLEKGE TDDATAMSYG FIPGVSRWSP
FHGSAYAVVE SLSKLLAIGA NPLTARLTFQ EYFERLKDVP ERWGKPAAAL LGAMEAQLKL
GIPSIGGKDS MSGTFETIDV PPTLVSFAVA MTKASKTVSA EFKNVGSKVI YVPVPENKET
LMPDWDKLIA MYKAVYKLFD EGKVLSASVV KEGGAAASVC KACFGNGYGF KFTNKLTNDE
LFAPLSGSLV LELADGAELD NSVVSYDLGT VTDDGKVTVN GAAVDVNTLI EKWTAPLEKV
FPTKAECPEI AVDIPLFTER NTSSPAIKTA KPTVFIPVFP GTNCEVDSAR AFEKAGANVE
LLIVKNLTSA HIEETIKAME KIISKSQMIM FPGGFSGGDE PDGSGKFIAT TFRNPRIANA
VNEMLKNRDG LMLGICNGFQ ALIKLGLVPY GEIRELKPTD PTLTFNTIGR HISHMAYTRV
TSVKSPWFAS VNAGDVFAIP VSHGEGRFMA DEATVKMLAE NGQIATQYVD LNGNPSADIT
YNVNGSVCAI EGITSPDGRI LGKMGHSERK GDSLYKNVPF AKDQLIFESG VKYFK
//
