ID R5LP41_9CLOT Unreviewed; 1254 AA.
AC R5LP41;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:CCY80948.1};
GN ORFNames=BN500_00655 {ECO:0000313|EMBL:CCY80948.1};
OS Clostridium sp. CAG:149.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262776 {ECO:0000313|EMBL:CCY80948.1, ECO:0000313|Proteomes:UP000017912};
RN [1] {ECO:0000313|EMBL:CCY80948.1, ECO:0000313|Proteomes:UP000017912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:149 {ECO:0000313|Proteomes:UP000017912};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY80948.1}.
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DR EMBL; CAYX010000008; CCY80948.1; -; Genomic_DNA.
DR AlphaFoldDB; R5LP41; -.
DR Proteomes; UP000017912; 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: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; 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
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:UP000017912}.
FT DOMAIN 179..228
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 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; 139075 MW; 1CE7F5526EB57253 CRC64;
MSVRRIFVEK RPEFAVKAKE LRDEIESYLG IKTVTGVRVL IRYDIENVSE AAYREALSTI
FSEPPMDDVY EESFETGEGD TVFTVEYLPG QFDQRADSAE QCVKLLSEEE EPIIRSATTY
VVSGTLTEEE KAAVKSLCIN PVDSRENNNP KPETLVAVFE QPEDVKIFAG FMDMPKEELK
SLYESLNLAM TFKDFLHIQN YFKNEEKRDP SVTEIRVLDT YWSDHCRHTT FQTELKDVEF
TKGDYNEPIE NTYRQYLADR EELYAGRSDK FVCLMDLALM AMKKLRKEGK LQDMEVSEEI
NACSIVVPVV IDGKEEEWLV NFKNETHNHP TEIEPFGGAA TCLGGAIRDP LSGRTYVYQA
MRVTGAADPT RPMSETMHGK LPQRRIVTDA AHGYSSYGNQ IGLATGYVKE IYHPNYAAKR
MEIGAVMAAA PRKNVIRETS DPGDVIILMG GRTGRDGIGG ATGSSKVHTE ESIEVCGAEV
QKGNPPTERK LQRLFRRPEV SRLIKKCNDF GAGGVSVAIG ELAAGLEIDL DKVPKKYAGL
DGTEIAISES QERMAVVVDK KDVEQMMAYV AEENLEAVPV AVVTESPRLV MHWRGKTIVD
ISRAFLDTNG AHQEASVTVE VPTREGNVFE RKEIGDVREH WLKLLSGLNV CSQKGLVEMF
DASIGAGSVF MPYGGKYQLT ETQAMVAKLP VLEGKCDTVT MMSYGYDPYL SSWSPYHGAV
YAVLDSVAKI AANGGDFKKI RFTFQEYFKR MTEDRTRWGT PFSALLGAYS AQMGFGLPSI
GGKDSMSGTF NDEVHGEINV PPTLVSFAVD ISDKQHVVTP EFKKAGSKIV VMKIEKDGYD
LPVYSQVMDS YEKLYRDMEA GNIISAYAVE AGGIAEAVSK MAFGNKLGVK VEHNVDPRDF
FAPGWGNIVC EVPDGKVGNL GITYTVIGEV TDRAAFEYGN VTISMDEALN AWTRTLEDVF
ATESGVEQKE VRTEIYNTDK VYICKNKVAK PRVFIPVFPG TNCEYDSAKA FERAGAEVIT
KIFRNRDAAD IRDSVEVYKK AIAQSQIVMF PGGFSGGDEP DGSAKFFATT FRNAVLKEEI
EKLLNERDGL ILGVCNGFQA LIKLGLLPEG RITELKSDSP TLAMNTIGRH ISKMVNLKVV
SNKSPWLREA ELGGIYVNPV SHGEGRFVAS SEWIEKLYAN GQVATQYVDA EGRPTMDEAW
NPNGSMMAIE GITSEDGRIY GKMAHSERIG DGVAVNIYGN QDIKIFESGV KYFQ
//
