ID B0PFX9_9FIRM Unreviewed; 1235 AA.
AC B0PFX9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:EDS09567.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:EDS09567.1};
GN ORFNames=ANACOL_03711 {ECO:0000313|EMBL:EDS09567.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS09567.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS09567.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS09567.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS09567.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS09567.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS09567.1}.
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DR EMBL; ABGD02000027; EDS09567.1; -; Genomic_DNA.
DR RefSeq; WP_006876568.1; NZ_DS544188.1.
DR AlphaFoldDB; B0PFX9; -.
DR STRING; 169435.ERS852551_00261; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_003100_2_0_9; -.
DR Proteomes; UP000003803; 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; 1.
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:EDS09567.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 184..228
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 437..588
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1076
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1235 AA; 133865 MW; A7DC3A1D34D76BFB CRC64;
MSVYRIYVEK KQPFAVEAAG VLADIRTVLG LGCVERVRIL NRYDVEHIDE ADFQSARSTI
FSEPQVDLTY DELPAPAENE RVFAVEYLPG QFDQRADSCA QCIALAFAKP RPAVRTARVF
ILSGQIGGEA LEQIERYLVN PVESRLASLE KPKTLDTRYD IPTTVETLDG FTELDAAGLR
GFVEQYGLAM DESDIAFCQD YFKNTERRDP TITEIRMIDT YWSDHCRHTT FLTHIENVRI
ETPYIRESFE KYQKLRAELY ADKDKPMTLM DLAVIGAKAL RAQGLLGDLD ESEEINACSV
KIKVDVDGED QDWLLMFKNE THNHPTEIEP FGGAATCLGG AIRDPLSGRS YVYQAMRVTG
AADPTVPLSE TLPGKLPQRK IVTTAAAGYS SYGNQIGLAT GHVAEVYHPG YAAKRLEIGA
VIGAAPAAHV VRERPVPGDI VILLGGRTGR DGCGGATGSS KSHTLQSLES CGAEVQKGNP
PIERKLQRLF RNGEATRMIR RCNDFGAGGV SVAVGELADG LRINLDAVPK KYDGLDGTEL
AISESQERMA VVVAPEHVEP FIALARAENL EATVVAEVTA EPRLVMDWNG RKIVDLSRAF
LNSNGAPKRT DIEIEPPLAY ARPRSEAPLR EKWLSMMGDL NVCSQKGLVE RFDSTIGAGT
VLMPFGGEAQ LTPAQAMAAK IPVPGGETTT VSLMGWGFNP GACAASPYHG AMDAVVESVA
KIVAAGGSRR RCWLTFQEYF ERTKNDPKRW GKPMAALLGA LEAQLQLGIG SIGGKDSMSG
TFESLDVPPT LVSFAVSVAN QANIISPEFK HAGSRVYLLA PAYDEYRLPV FESVKAVFDT
VERLIAEKRV VSAWTLGYGG VCEGVTKMCF GNRLGFDFAA TFDDAALFEP MYGAFLLEAP
EPIEGLACIG TVSPAYTIRY GFDLLPLDDI QEEWEERLQP VFPYLKPTGG SAPVYSAAPA
APQRAAVSVA RPRVLIPVFP GTNCEYDTAR AFERAGARAD IFVVRNLTAA DIAESAAAFS
EAVGRAQIIA LPGGFSGGDE PDGSAKFITA FLRGPAVRDA VMELLKNRDG LMCGICNGFQ
ALIKLGLVPY GEIRDMDENC ATLTYNSIGR HQSMLVRTRI ASNRSPWLAG MSVGDIHTIA
ISHGEGRFVA PPALLETLAQ NGQIATQYVD PDGQPTLDIR YNPNGSIGAV EGITSPDGRV
LGKMGHSERS GGGLYKNVPG DKFQDLFSGA VRYFQ
//
