ID A0A1S8M9P7_9CLOT Unreviewed; 1255 AA.
AC A0A1S8M9P7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:OOL86785.1, ECO:0000313|EMBL:URZ11883.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:OOL86785.1, ECO:0000313|EMBL:URZ11883.1};
GN Name=purL {ECO:0000313|EMBL:OOL86785.1};
GN ORFNames=CROST_026000 {ECO:0000313|EMBL:URZ11883.1}, CROST_23850
GN {ECO:0000313|EMBL:OOL86785.1};
OS Clostridium felsineum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=36839 {ECO:0000313|EMBL:OOL86785.1};
RN [1] {ECO:0000313|EMBL:OOL86785.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:OOL86785.1};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:URZ11883.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:URZ11883.1};
RA Poehlein A., Schoch T., Duerre P., Daniel R.;
RT "Genome sequence of C. roseum typestrain.";
RL Submitted (APR-2022) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LZYV01000076; OOL86785.1; -; Genomic_DNA.
DR EMBL; CP096983; URZ11883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8M9P7; -.
DR STRING; 84029.CROST_23850; -.
DR KEGG; crw:CROST_026000; -.
DR Proteomes; UP000190951; 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; 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; 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:OOL86785.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 181..230
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 443..595
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1096
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1255 AA; 139809 MW; 27A24E27F5152924 CRC64;
MNKKVRRIFV NKKAGFDVAA KALLKDLVEN LGIKALEDLS ILNRYDVSGI DDSEYEEAKK
IIFSEKTVDD VYDEAFMLES EDKVFAVEYL PGQYDQRADS ACQCIKILTG NEEVLINSAK
VIILKGNISD TDFNKIKKYV INPVDSREAS LDKAETLEVT YDLPYEVEII EGFTNMSDTE
LEKFLKTNGL AMSMEDLKFC QGYFKNEEER NPTITEIKVI DTYWSDHCRH TTFQTRLNNI
KFEDGKYSDI LKDAYKNYVD ARKYVYEDRE KEVCLMDIAV IGMKELKKKG FLNDLDESEE
INACSIVVDA DVNGKDEKWL VMFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRSYVYQ
AMRVTGSGDP RTKIEDTTKG RLPQKKITLE AAHGYSSYGN QIGLATGQVS ECYDEGFIAK
RMEVGAVVGA APKENVVREI PEPSDVVILL GGRTGRDGCG GATGSSKEHD VNSLQNCGAE
VQKGNAPTER KLQRLFRNKE VSTLIKRCND FGAGGVSVAI GELTEGLDIN LDLVPKKYEG
LDGTELAISE SQERMAVVVR KKDAEKFMEY ADKENLEAVI VANVTDTKRL KLFWKGNAIV
NVSRAFLDTN GVRQNVDVFV KAPKEKENYF KGKENKKVTR EAVLSELRDL NVCSQKGLSE
RFDSTIGAGT VLMPFGGKYQ ITPAEGMAAK LPVLEGDTTT GTVMTYGYNP KIGKWSPFHG
AMYAVIESLT KLVCMGGDYR KARLTFQEYF ERLNKEPEKW GKPFAALLGA LKAQEVFKTP
AIGGKDSMSG TFMDLNVPPT LVSFAVNVVN INNVISPEFK KVGSKLVLLK CERDENEVPI
FDKLKRNFDI TVELIKSKNV LSAQSIRHGG LIEAISKMCF GNKIGFEMVG EESLFEPDYG
SILLEIPEAL DLKEIFKDID YKVVGSTIEE DKIILKDFSI ELKDALEAYT EPLEKIFPTK
AETESKINLS LYDEIKAKEV ERKSPLIKVA RPRVFIPVFP GTNCEYDSSR AFERAGAEVS
TFVFRNMKTS DIEDSINKMV KEINKSQIIM LPGGFSAGDE PDGSGKFIAA VLRNEKIKES
VAKLLNTRDG LMLGICNGFQ ALIKLGLVPY GEIKEITKEC PTLTYNNIGR HVSQIAYTKI
VSNKSPWLSN VKNGDIHSIP ISHGEGRFAA SREVVENLIK NDQIATRYVD LNGNSSYETE
VNPNGSVLCI EGITSPDGRI LGKMGHSERF SRGTYKNIVG NQDQKIFESG VQYFK
//
