ID A0A1E8VVR9_9ACTN Unreviewed; 1243 AA.
AC A0A1E8VVR9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:OFK23872.1};
GN ORFNames=HMPREF2826_03730 {ECO:0000313|EMBL:OFK23872.1};
OS Olsenella sp. HMSC062G07.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1739330 {ECO:0000313|EMBL:OFK23872.1, ECO:0000313|Proteomes:UP000176754};
RN [1] {ECO:0000313|Proteomes:UP000176754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC062G07 {ECO:0000313|Proteomes:UP000176754};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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:OFK23872.1}.
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DR EMBL; LTFF01000025; OFK23872.1; -; Genomic_DNA.
DR RefSeq; WP_070639322.1; NZ_KV806951.1.
DR AlphaFoldDB; A0A1E8VVR9; -.
DR STRING; 1739330.HMPREF2826_03730; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000176754; 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; 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; 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:UP000176754}.
FT DOMAIN 182..225
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 433..584
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 1207..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1084
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1243 AA; 133690 MW; CEE88E4C16C0F853 CRC64;
MVSRVYVEKK PGFDVKARQL RRELADVLGI RGLTGLRLVN RYDVEGIDEE LFRRCVPLVF
SEPQSDVASL ELPDAHGAQL FAVEFLPGQF DQRAASASEC IQLISQGERP VVASATLYYL
EGNLSAKDVA AVKGYVINPV EAREASLDAR PTLKSSYPVP DDVEVLDGFD ALSPDELAAF
IKDRGLAMDL ADVSFCQEYF KGEGRPPTIT EIKMIDTYWS DHCRHTTFGT RLERVAIDDA
TVRQAFDAYL DMRRELGREG RPICLMDMGT IGAKWLKARG VLANLDESEE INACTVKVKV
DVDGTDEDWL FLFKNETHNH PTEIEPFGGA ATCIGGAIRD PLSGRSYVYQ AMRVTGAGDP
LAPVSQTMRG KLPQRKLVTT AAEGYSSYGN QIGLATGQVS ELYHPGYVAK RMEIGAVVGA
TPASHVRRET PAPGDKVILL GGRTGRDGIG GATGSSKAHN VDSLAKDGAE VQKGNAPEER
KLQRLFRRKD ACRLIKRCND FGAGGVSVAI GELADGLTID LDRVPKKYEG LDGTELAISE
SQERMAVALA AKDVDEFLGY AREENLEATV VAEVTARPRL TMTWRGATIV DVSRAFLSSN
GAPKHQDVHV VAQGSWQPVW EGRTLEERLR ALVTDKNVAS NKGLAERFDA TIGAASVLMP
FGGATQLTPA LAMAAKLPTD GETTTCSGMA WGFNPFLTSA NAFTGAYLAV VESLCRLVAT
GFAHEDAYLT FQEYFERLRD VPERWGKPVA ALLGALMAQR DLGVGAIGGK DSMSGSFEDL
DVPPTLVSFA TALGTVGCVT SPELKGAGHR LVLVRPAYLD DGITPRSESL LSAMSLVERL
IHSKGALAVS TPGYGCLAEA LFKMCVGNQL GMRLSDDLDE GELFSPAYGS FVVELAEGAT
VTSPCADDVE LRALGETTAA YALVVAGQMI DLAGLQEAWE ATMEPVFAYR RAGEPEEPVS
FDASRRHVSR PAPLVKTARP RVVIPVFPGT NCEFDSARAF ERAGAEAHAL VINNLTPDSV
AQSTQALVDE IAQSQILMIP GGFSGGDEPD GSAKFITAFF RAPQVTEAVR DLLQARDGLV
LGICNGFQAL VKLGLVPYGD IVPMTADCAT LTFNAIGRHQ SRLVFTRVSS NLSPWLSRCE
VGDVHRIAVS HGEGRFVAPE PLIRELGERG QIAAQYVDAQ GLPSMDLSVN PNGSAWAIEA
VTSPDGRVLG KMGHSERSTP GTFKNVPGEH YQPIFEGGVA YFS
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