ID B1C1P7_9FIRM Unreviewed; 1253 AA.
AC B1C1P7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:EDS74839.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:EDS74839.1};
GN ORFNames=CLOSPI_01154 {ECO:0000313|EMBL:EDS74839.1};
OS Thomasclavelia spiroformis DSM 1552.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS74839.1, ECO:0000313|Proteomes:UP000004910};
RN [1] {ECO:0000313|EMBL:EDS74839.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74839.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS74839.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74839.1,
RC ECO:0000313|Proteomes:UP000004910};
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 (FEB-2008) 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:EDS74839.1}.
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DR EMBL; ABIK02000008; EDS74839.1; -; Genomic_DNA.
DR RefSeq; WP_004609687.1; NZ_DS562849.1.
DR AlphaFoldDB; B1C1P7; -.
DR STRING; 428126.CLOSPI_01154; -.
DR GeneID; 67386463; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_003100_2_0_9; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000004910; 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:EDS74839.1};
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:UP000004910}.
FT DOMAIN 181..229
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 444..592
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1091
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1253 AA; 139052 MW; 1C21D708A34A85CF CRC64;
MSDVKRIYVE KRTAYATEAN EIKHNLIEQL GLEIKTLRVI NRYDVQGISD DILNKGIDTI
LSEPMVDDVY QEDFPKNEEE AIFAIEFLPG QYDQRADSCE QCFAILTGNT NAKVKCARVF
AITFAGNKDD VLNKIQGFLI NPVDQRLASL DKPKNLNDEV PEIKPVSTIT GFNEFSKEEL
EKFLVDNGMA MNYDDLKVTQ DYFKNEEKRD PTETELKVLD TYWSDHCRHT TFATVITDLD
IENGAFKEIL EKDIENYKTS RHLVYGIDTK RPLTLMDLAT ISMKELRKTG YLDDLEVSEE
INACSVEITV HTTDGDEQWL LMFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRAYVYQ
SMRITGAGDP RKSLEETIKG KLPQRKICQE SAHGFSSYGN QIGLTTGYVH EIYDEGYVAK
RMELGAVVAA APKEQVKRLE PLKGHVVLLI GGRTGRDGIG GATGSSKSHD IKSIETAGAE
VQKGNPVEER KIQRLFRNKE VSEKIVRCND FGAGGVCVAV GELAPGLEID LDAVLKKYDG
LTGTELAISE SQERMAIVVD SKDVDFIKAE CAKENLEVVQ VAIVTDQNRL IMRHMGKDIV
NISREFLDAA GAKRYQDVKI MLPDFENTPF DKQPQTSFVD TVTKTLSKLS VASQKGLIER
FDSSIGNGTV LSPFGGIKYH SETEGMAALI PVLGKETTTA SIMTYGYNPV ISKWSPYHGS
IYAIVESIAK IVAMGGNYHN IRFSFQEYFE KLLTNPTTWG KPTAALLGAY RVQNALKLPS
IGGKDSMSGS FEDLHVPPTL VSFAITSSDV DDIMTPEIKE AGHILVEVVI NKDKYHVFDF
DHLQKQYDAI MALMKENKIY SAYTVKDGGV IEAVSKMAFG NGIGVAFSGE YDLDSYVMRD
YGNIIIEVKN EEDLDVFDNY RIVGTTNDSE VLSYGHEAIS LDEAYAINKA PLESVYPTRE
VAPTSEIKVA ACNTRSTLKA KVTVETPLVV IPVFPGTNCE YDSKRAFEKA GAKVQLVLIR
NKTEQMLTDS INELEAAIRQ ANIVMLPGGF SAGDEPEGSG KFIATVLKNP RLKDAISDLL
DNRDGLMIGI CNGFQALIKL GLLPYGKIQD MSKDDPTLTF NTIGRHVSQM VDTRIGSVKS
PWLKYVNVDD IHTIPVSHGE GRFVAPKEVI EELFENGQVF SQYVDPNRKV TMQTPYNPNG
SMYAIEGIIS RDGRVIGKMG HSERQGENRF KNVYGEMDQK LFEAGVDYFK GGK
//
