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Database: UniProt
Entry: A0A134CF39_9FIRM
LinkDB: A0A134CF39_9FIRM
Original site: A0A134CF39_9FIRM 
ID   A0A134CF39_9FIRM        Unreviewed;      1260 AA.
AC   A0A134CF39;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:KXB90800.1};
GN   ORFNames=HMPREF3191_01119 {ECO:0000313|EMBL:KXB90800.1};
OS   Veillonellaceae bacterium DNF00626.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae.
OX   NCBI_TaxID=1588754 {ECO:0000313|EMBL:KXB90800.1, ECO:0000313|Proteomes:UP000070542};
RN   [1] {ECO:0000313|EMBL:KXB90800.1, ECO:0000313|Proteomes:UP000070542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00626 {ECO:0000313|EMBL:KXB90800.1,
RC   ECO:0000313|Proteomes:UP000070542};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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:KXB90800.1}.
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DR   EMBL; LSDR01000065; KXB90800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A134CF39; -.
DR   STRING; 1588754.HMPREF3191_01119; -.
DR   PATRIC; fig|1588754.3.peg.1090; -.
DR   Proteomes; UP000070542; 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:UP000070542}.
FT   DOMAIN          190..238
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          451..603
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   1260 AA;  139121 MW;  68115FBAF3717422 CRC64;
     MLVNGESKGD GVILTHIRRL YVRKKEGFRG NEAGVLAEMR EVLGEHIKSV AIYHRYDVAH
     ISDENYEKAI GTIFSEPPVD EVTETLPKGD YLVAVELLPG QYDQRADSAE QCLSVLTGNN
     GASVLCALVY AFTGSFTKED KEKIVKYLIN PVESFKADLG EVDEIDMPWE KPDEVEHIQN
     FISKDDESLR KMLSDLGLAM SFDDLRMIYD YFKNEEKRDP TITEIRVLDT YWSDHCRHTT
     FSTKLNDIVV DDGVFTKPIQ KALAMYEETR DQIYGSDACR PMTLMDMATI AVKDLKKHGF
     LGNLDSSEEV NACTIKITVD TPTGKEDWLL LFKNETHNHP TEIEPYGGAA TCLGGCIRDP
     LSGRAYVYQA MRVTGAADPA TPLKDTLPGK LPQRKIVMES AKGYSSYGNQ IGLATGEVKE
     YYHPGFMAKR MEIGAVIAAT PADHVVRKEP EPGDVIILVG GRTGRDGMGG ATGSSKELDT
     TSIETCGAEV QKGNPLIERK IQCLFRRKEV TRLIKRCNDF GAGGVSVAVG ELADSLLINL
     DKISKKYEGL DGTELAISES QERMACVVRK EDAERFIAYA AEENLEATVI AQVTGSGRLV
     MTWQDDVIVD ISRAFLNTNG AMQETDVHIV APNEDSYFKK NEIDDIEKNW INVMSDLNTA
     SQQGLAEHFD ATIGAGTVLM PFGGAYQKTP TDGMVAKVPI RFGETDTASF MTHGFDPYLA
     TWSPFHGAVY AILLSLTRLV SLGADWRKAY LTLQEYFEKL RDKSTWGKPT AALLGAFYAQ
     HELGIAAIGG KDSMSGTFND LHVPPSLISF AVAPGKASEA VSQELKEKGD CLILFGMPKD
     EMGMPDWNVF KKHSDFLYEE VQKGNIRAMK AVGHGGVAAT VAEMAFGNHL GVTFSDELPI
     FKYFNNFYGA IVVETTKTLA EKYREQPHTK ILGIVGGDSM VLGNEAISLD KLLKAYEHTF
     DWIFPREAES LAGTIPKVEE HAAVRDIHVR TKSITPKVFI PTMPGTNCEI DSARAFERAG
     AATDIFILRN RDAAELRESV QEMVRRIKEA QIIMFPGGFS AGDEPDGSGK FIATVFRNDT
     LVEALDGLLH QRDGLILGIC NGFQALIKLG LVPYGACQPL TKEAPTLTFN TIGRHISRYV
     TTKVLSNRSP WLSLCRTDEL YQIPISHGEG RFIASDEQIQ TWMKQGQIAT VYTDEKGNIS
     YDSRYNVNGS AWAIEGITDP TGRIFGKMGH SERYGKNIGK NISGNKEQPI FLSGVTYFKG
//
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