ID C4GAG6_9FIRM Unreviewed; 1266 AA.
AC C4GAG6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:EEP28109.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:EEP28109.1};
GN ORFNames=GCWU000342_00917 {ECO:0000313|EMBL:EEP28109.1};
OS Shuttleworthia satelles DSM 14600.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Shuttleworthia.
OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP28109.1, ECO:0000313|Proteomes:UP000003494};
RN [1] {ECO:0000313|EMBL:EEP28109.1, ECO:0000313|Proteomes:UP000003494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP28109.1,
RC ECO:0000313|Proteomes:UP000003494};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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:EEP28109.1}.
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DR EMBL; ACIP02000002; EEP28109.1; -; Genomic_DNA.
DR RefSeq; WP_006905928.1; NZ_GG665866.1.
DR AlphaFoldDB; C4GAG6; -.
DR STRING; 626523.GCWU000342_00917; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_003100_2_0_9; -.
DR Proteomes; UP000003494; 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; 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:EEP28109.1};
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:UP000003494}.
FT DOMAIN 178..227
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 441..592
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1107
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1266 AA; 140983 MW; 3BF60BE3FCCC65F7 CRC64;
MGAVRRLYVE KKRSYAVAAR ELEAEIKSYL GIRTVDKVRI LIRYDLENVS DAVYQQAVKT
VFAEPPVDDV YEETFERTGV SFSVEYLPGQ FDQRADSAEQ CLKLLNEDEE PIIRTATTYI
IEGKIRPEEL EEIKNHCINP VDSRECADDK PQSLDIKYKE PDDVIVFQGF SSMGEKPLRE
LYESLNLAMT FRDFLWIQTY FAQEEKRDPS MTEIRVLDTY WSDHCRHTTF STELTHVKIP
DGFYAEPIRK TFDEYKDNYR ILYQDRDDKF VCLMDIALAG AKILKKKGLL TDQEESDEIN
ACSIVVPIEV DGQTEEWLVN FKNETHNHPT EIEPFGGAAT CLGGAIRDPL SGRTYVYQAM
RVTGAADPTV SVKETLKGKL PQKKIVREAA QGYSSYGNQI GLATGYVKEI YHPDYVAKRM
EIGAVMGAAP RRAVQRLNSD PGDRIILLGG RTGRDGIGGA TGSSKAHNTE STQECGAEVQ
KGNAPTERKL QRLFRREEVS YIIKKCNDFG AGGVSVAIGE LADGLDINLD LVPKKYAGLD
GTELAISESQ ERMAVVVAPE NVDRFLSYAA EENLEAVEVA VVTVSPRLVL RWRGKKVVDL
SRAFLNTNGA HQETSVEVVL PEEKDNYTEK IAVSAVREAL EANDVRAAWL ALLSDLNVAS
QKGLVERFDG SIGTGSVFMP FGGRYQLTET QSMVAKLPVS GKRSSAVSMM AYGYDPYLSK
WSPYHGANFA VLDSLARIVA SGGDYHKIHF TFQEYFGRMS EDPRRWSQPF TALLGAYHAQ
LRLGLASIGG KDSMSGSFNE IDVPPTLVSF AVDVADLSDI ISPEFKRAGD DIVLFQAKRD
PYDLPDYEQI MRLYDAFARL IKDGVVRSAY TLDAYGAACA MSKMAFGNRM GFVLDQKLRR
EDLFAFATGS LLAEIDPAKK ERMEEILIAH GLTDACSRLG QLTDDGRFVF GDMDLSVDEA
IGAWTRPLEK VFPTRSGQET DRIESPVYRA KRIYVNQNKV ARPTVFIPVF PGTNCEYDSA
DAFEKAGAKT LVKVFRNRNA QDIRESVDAF ARAIEKAQIV MFPGGFSAGD EPEGSAKFFA
TAFRNEKMKE AVNKLLSERD GLVLGICNGF QALIKLGLVP CGQIQAQTEE SPTLTYNTIG
RHISKEAYIK VVSNKSPWLQ EADLGGVYTN PASHGEGRFV ASKDWLDRLF ANGQVATQYA
DMEGNISMDE EYNINGSYMA VEGITSPDGR VFGKMCHSER QGRGVAVNIY GQQDMRIFES
GIKYFH
//
