ID I9NLI6_9FIRM Unreviewed; 1254 AA.
AC I9NLI6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:AJQ29512.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:AJQ29512.1};
GN ORFNames=JBW_04181 {ECO:0000313|EMBL:AJQ29512.1};
OS Pelosinus fermentans JBW45.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1192197 {ECO:0000313|EMBL:AJQ29512.1, ECO:0000313|Proteomes:UP000005361};
RN [1] {ECO:0000313|EMBL:AJQ29512.1, ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|EMBL:AJQ29512.1,
RC ECO:0000313|Proteomes:UP000005361};
RX PubMed=26404608;
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Elias D.A., Arkin A.P.,
RA Fields M.W., Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45, a Member of a
RT Remarkably Competitive Group of Negativicutes in the Firmicutes Phylum.";
RL Genome Announc. 3:e01090-e01015(2015).
RN [2] {ECO:0000313|Proteomes:UP000005361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBW45 {ECO:0000313|Proteomes:UP000005361};
RA De Leon K.B., Utturkar S.M., Camilleri L.B., Arkin A.P., Fields M.W.,
RA Brown S.D., Wall J.D.;
RT "Complete Genome Sequence of Pelosinus fermentans JBW45.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP010978; AJQ29512.1; -; Genomic_DNA.
DR RefSeq; WP_007960360.1; NZ_CP010978.1.
DR AlphaFoldDB; I9NLI6; -.
DR STRING; 1192197.JBW_04181; -.
DR KEGG; pft:JBW_04181; -.
DR HOGENOM; CLU_003100_2_0_9; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000005361; 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: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; 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:AJQ29512.1};
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:UP000005361}.
FT DOMAIN 186..230
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 443..593
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1095
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1254 AA; 137562 MW; D20D8F926A0D63DF CRC64;
MPYEVKRIFV EKRQDFAVEA KGMYADLTEN LGITGLKHVR LVNRYDISGI SQEEFVEAKQ
SIFSEPTVDD VYDEILTIEP EDKIFAVEYL PGQYDQRAHW AAQCVQILTK TENLSIRTAK
VIVLQGNITE DEFKKIKEYS INPVEAREAS LEKPRSLELT VEKPADVKTI PGFITQSAEE
LELLLKDMGL AMGLGDIAFC QQYFRDVEKR NPTITEIRVL DTYWSDHCRH TTFFTAIENV
DIGTGHFSEP IAKAYDQYRK ARSLVYKDRQ KDICLMDIAV MGMKELRLQG KLTDLDDSEE
INACSIVVPV DVDGSIEEWL VMFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRSYVYQ
AMRVTGSGDP RTKVEDTLAG KLPQRKITLG AAAGYSSYGN QIGLATGQVA EIYHEGFIAK
RMEIGAVIAA APKENVVRER PAVDDIVVVL GGKTGRDGCG GATGSSKEHT EESLATCSAE
VQKGNPPTER KIQRLFRNPK ASQMIKRCND FGAGGASVAI GELTDSLVID LDALPKKYAG
LDGTELAISE SQERMAVVIA PYHLEEFMSY VAIENLEAAV VAKVTDTGRL VMLWRGIPIV
DISREFLNTN GVKQKVDVQV TAPVEAENYF AAKTNDAEAL ETAWFDNLRD LNVCSQKGLV
EMFDSTIGAS TVLMPFGGKF QTTPAEGMAS KIPVLKGNTN TATLMTYGYD PQLTTWSPFH
GAVYAVVEAV AKIVAMGGEY HTVRLTLQEY FERLGQDAVK WGKPFSALLG ALHAQEQFSI
PAIGGKDSMS GTFKELTVPP TLVAFAVNVV QADRVISPEF KEIGSQIIQV PLIRDAYELP
DFPVVCQNYA NITQLIKAGH VLAAHTIKRG GLAAAISKMS FGNKIGMVFT SPLSSQDLFA
ADYGSLILEI PSGIAVKEML GEMTYSVIGH TQEQPRIDIN GYSIDLEKAQ TAWEQPLTKV
FATQTEISKE KPKQELFASN PKKAKHSFAK PRIFIPVFPG TNCEYDSAKA FEMAGGIVDT
MVIRNLTPSA VEESIEEMVK SIDQSQIIML PGGFSAGDEP DGSGKYIATM FRNPKIKEAL
REFLSQKDGL MLGICNGFQA LIKLGLVPYG DIVDLSPECP TLTYNQIGRH ISCMANTKLV
SKLSPWFNNI ELGEVHTIPV SHGEGRFVAS SAVLNSLRQK GQIATQYVDE TGQPTYDIRY
NPNGSVEAVE GITSPDGRIL GKMGHSERIG NQVVKNVPGS KDQQLFAAGI GYFR
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