ID A0A133SJA3_9FIRM Unreviewed; 1247 AA.
AC A0A133SJA3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:KXA69754.1};
GN ORFNames=HMPREF3201_00741 {ECO:0000313|EMBL:KXA69754.1};
OS Megasphaera sp. MJR8396C.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1603888 {ECO:0000313|EMBL:KXA69754.1, ECO:0000313|Proteomes:UP000070314};
RN [1] {ECO:0000313|EMBL:KXA69754.1, ECO:0000313|Proteomes:UP000070314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR9396C {ECO:0000313|EMBL:KXA69754.1,
RC ECO:0000313|Proteomes:UP000070314};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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:KXA69754.1}.
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DR EMBL; LRVC01000023; KXA69754.1; -; Genomic_DNA.
DR RefSeq; WP_062411744.1; NZ_KQ958161.1.
DR AlphaFoldDB; A0A133SJA3; -.
DR STRING; 1603888.HMPREF3201_00741; -.
DR PATRIC; fig|1603888.3.peg.714; -.
DR Proteomes; UP000070314; 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; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 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; 2.
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}.
FT DOMAIN 179..228
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 439..590
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 835..927
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1087
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1247 AA; 135802 MW; EB35F9B60E56BDF8 CRC64;
MQSIRRLYVA KKGIFADEAK RLLTDLQENL LIKGLTDIHI FHRYDVSGLD DAAFEAAKNM
IFSEPPVDAV YDTLPTREGD TVLAVEYLPG QYDQRADSAV QCLQMLTMKN DSLVRTAQVI
VLSGDLSGTD ITAIKNYCIN PVEAREASLE PATSLELAWE KPADVPTVEG FISMDDAALT
DLSSQMGLAM SFDDLKFVQT YFRDEEKRNP TITEIRVIDT YWSDHCRHTT FMTELTDVSF
EKGTFTAPIQ RAYESYKTTR KNLNRKKPQT LMDMATIAVK ELKAAGKLDN LDESEEINAC
TIIIPVDVDG VEEEWLLLFK NETHNHPTEI EPFGGAATCL GGCIRDPLSG RSYVYQAMRV
TGAGDPRQVV QDTLVGKLPQ RKLTTGAAKG YSSYGNQIGL ATGEVKEYYN PGFVAKRMEI
GAVLGAAPRQ NVVREEPLPG DIIILLGGKT GRDGCGGATG SSKKHTVESL ETCGAEVQKG
NALTERKIQR MFRRQEVTTL IKRCNDFGAG GVSVAIGELT DGLDINLDKV PKKYEGLDGT
ELAISESQER MAVVVAPENV DKFMNYAAEE NLEATIVAVA TDTKRLVMHW RDQNVVNITR
AFLDANGVTQ RRKALVTAPE DTDFFKAAAV NDVAKTWLDT MGTLNIASEQ GLAERFDSTI
GARTVLMPFG GKYQKTPVEG MVAKIPVEHG NTTTASIFTH GYDPDLAIWS PFHGALYAVI
QSIAKLVALG GDRKKVYLTM QEFFQSLGQN ETAWGQPVSA LLGAFVAQQV MEVAAIGGKD
SMSGTFENLT VPPTLVSFAI APEHTDHIVS PEFKTAGDAV LLFDLPRDGE GMPDFDTFKQ
HCDFLHQAVV DGKVKAMHAV GQGGIAAAVA QMAFGNGIGF DIDADFAVQE LFNLRYGALL
VETDSETAAA WVKRDQVSLV GKTADAANIS VAGVKIALSD LQDAWEKPLN QIFPIKDKDG
EGDAELPLFT TYGPRRSESF GAPRVFIPVC PGTNCEYDSA AAFERAGATT DVMVLRNNTP
KDLAESIEEM AKRMAKAQII MFPGGFSAGD EPEGSGKFIA TLFRNPVLSE ALESLLYQRD
GLALGICNGF QALIKLGLLP YGKIQPLKAD SPTLTYNSIG RHLSRMVDTK VVSVMSPWFS
SCQAGDIHTV AISHGEGRFI ATPEQIRELA AKGQIATQYV DLSGKASNES EYNPNQSILA
VEGITSPDGR VLGKMAHTER FSADDIFKNI DGNKLQPIFT SGVNYFK
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