ID A0A410PN67_9CLOT Unreviewed; 1253 AA.
AC A0A410PN67;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:QAT40253.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:QAT40253.1};
GN ORFNames=EQM05_08270 {ECO:0000313|EMBL:QAT40253.1};
OS Clostridium sp. JN-9.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2507159 {ECO:0000313|EMBL:QAT40253.1, ECO:0000313|Proteomes:UP000287890};
RN [1] {ECO:0000313|EMBL:QAT40253.1, ECO:0000313|Proteomes:UP000287890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN-9 {ECO:0000313|EMBL:QAT40253.1,
RC ECO:0000313|Proteomes:UP000287890};
RA Ma S.;
RT "Draft genomes of a novel of Clostridium strains.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP035280; QAT40253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410PN67; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000287890; 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:QAT40253.1};
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:UP000287890}.
FT DOMAIN 183..229
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 442..593
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1094
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1253 AA; 139717 MW; 7DC5CCBA2A527CBE CRC64;
MKKRVNRIFV RKKPEYAVES HLLLQDLKLS LHLENLDDVK IINRYDIQGI SDEEYEISKK
TIFSEPNVDF IYEEKLPAFE NSKIFASEYL PGQYDQRSDS ASQCLQILTK KEDILVKYAK
VFIITGNIND EEFNKIRQYC INPVDSREAS LVKPDKIENL VNVPETVETI ENFISLNEDE
LNDFYKDKNL AMSFSDLKFV QSYFKSEKRN PTITEIKVID TYWSDHCRHT TFMTEIDNVE
FSDDDLTAPI KNTYKEYINS RDYVYGDKNK PKCLMDLAVI CMKELRKKGL LDDLEESEEI
NACSIEVEAE IDGKKEKWLV MFKNETHNHP TEIEPFGGAA TCLGGAIRDP LSGRSYVYQA
MRVTGSGDPT VSLDETLPGK LPQKKITLGA AQGYSSYGNQ IGIATGCVHE VYHPGYVAKR
MEVGAVIGAA PKKNVIREEP VEGDIIILVG GRTGRDGCGG ATGSSKKHTE CSLESCGAEV
QKGNAPTERK IQRLFRNEKV SKLIKRCNDF GAGGVSVAIG ELSDGLKINL DVVPKKYEGL
DGTELAISES QERMAVVVSK DKAEEFIHFA SLENLEATIV AQVTKEKRLK MYWNGTAIVD
ISRDFLNTNG VRQKTDVFVK APSNIGRFFK ASTNTDSIKD ELFNRLSQLN GCSEKGLVER
FDSTIGAGTV IMPYGGKYQR TPSEAMVAKL PVRHGNTTTA TAMAYGFNPY ICELSPYHGA
VYSVIESVCK IVAAGGNYKN IKLTLQEYFE KLGTEPETWG KPFAALLGAY KVQRELGIAA
IGGKDSMSGS FNDLDVPPSL VSFSVGIVNS SKAISPEFEK LGSKIVYIPA EIDEHYLPDF
NTLKTNLDKV SQLINDGKVI SAQSIKNNGI LYAITLMCFG NKIGFNFTEN IKKDDLFNAE
YGAFILEFNS DTDIAEELKE INYKIIGSTQ SEPFIEIGKE KISIDDAYYA WSHTLEDIFK
TESEKITMDI EDIKFEYRSK KAPYIKIAKP RVFIPAFPGT NCEYDSEKAF INAGAEVNTF
IFRNLSSQDV SDSIKAMAEE IKKSQIIMIP GGFSAGDEPD GSGKFIANVF RNSEIKEAVM
ELLKNRDGLI LGICNGFQAL IKLGLVPYGE ITDIDEDSPT LTYNKIGRHV STMVNTKVTS
VLSPWLSKVN VGDIHTIPVS HGEGRFVASQ NFMKKLIENG QIATQYVDFR GHATYDINYN
PNGSYFAVEG ITSPDGRIFG KMAHSERMGI DICRNIPGNK DQKIFQSGVE YFK
//
