ID A0A140DR90_9FIRM Unreviewed; 1231 AA.
AC A0A140DR90;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AALO17_00330 {ECO:0000313|EMBL:AMK53167.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK53167.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK53167.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK53167.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011391; AMK53167.1; -; Genomic_DNA.
DR RefSeq; WP_067553945.1; NZ_CP011391.1.
DR AlphaFoldDB; A0A140DR90; -.
DR STRING; 1702221.AALO17_00330; -.
DR GeneID; 78476957; -.
DR KEGG; fro:AALO17_00330; -.
DR PATRIC; fig|1702221.3.peg.32; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000069771; Chromosome.
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; 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.
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:UP000069771}.
FT DOMAIN 172..219
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 430..581
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 446..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1231 AA; 134920 MW; 772E68173A7E5DDF CRC64;
MNTRIFVRKK PGFRVESRSL EDELRQSLNL PEEFRLLKYN IYDIFGADEE EVSLLKQHVL
AEAVTDEIAE PEGEDMIAFE FLPGQYDQRA DSAMQCLMLL SGRKPAVIRS GTLLEMENVT
EAQKEAIAAY VINPVESRRK DLTVLDNDQD VQVEPVPVIE EFTGMDEQAL TALHDRLGLA
MSLEDLAFVQ GHFRDDEHRD PTMTEIRVLD TYWSDHCRHT TFETVLEDVV FEKNRLHKRL
QEAYENYLDL RNKVHGGRKE STLMDMASLV GKYMRKTGQL EDLEVSDEIN ACSIEITVDE
DGVNTPWLLM FKNETHNHPT EIEPFGGAAT CIGGAIRDPL SGRSYVYQAM RITGAGDINR
PVSETMEHKL PQSKISRTAA RGYSSYGNQI GLPTTFVEEI YDDGYTAKRM EVGAVIGAAP
KSHVKREKPQ PGDFVVLIGG ATGRDGIGGA TGSSKEHTDT SLEKCSSEVQ KGNALTERKL
QRLFRNPEVT RRIRKANDFG AGGVSVAIGE LADGLVIDLD AVPVKYEGLD GTELAISESQ
ERMAAVIPAE EFEAFRELCR QENLDCVQTA VVTEEPRLVM NWRGKTIVDL PRAFLDTNGV
RQHQKVVVTA SDYDDDPFAP ARETTLTEVL KRPDVACQIG LAEMFDGSIG KSTVLMPFGG
RKQLTPEEGS VQKLPVDGFT NTVSAMTFGF DPVVAKCSPY LGAAYSVVAA LARQAALGMD
PLSARLSNQE YFERLGKDPV KWGRPLEAML GLIDAQMAFG TPSIGGKDSM SGTFNDIHVP
PTVITFAVTT GQADEVKPAE FAGAGHDLYL LAHRPLADGS PDYEQLKDSF RALRQAAPKV
LAARSVNNGG IAAALAKMAF GNWIGADVTV DDPWGFGIGS VIVEASEPLE DGRFEKIGQT
TADETVTING QTTALQDAFD AWTSTYEGLY PRKAADGEGQ PAADLVQGEK QYAGTRVEKP
QVLIPVFPGQ NCELDTARRF ERAGAQVKQF VLNDRTPEAL NESVDQLADE IRKAQILMIV
GGFSAGDEPD GSGKFIANVL KNPKIAAAVE AMRKENDGLI LGICNGFQAL IKSGLLPGGD
RLQGKDAPTL FRNDIDRHVS RIARTRITST KSPWLQDFKP GQVHSVAFSH GEGKFVADEE
TLKQLAASGQ IATQYVDDTG KPSMMGEDNI NGSAWAVEGI TSEDGRVLGK MGHSERWEEG
LFINIDGDKD QDIFASGVRF FTRNPLPDEN T
//
