ID U2T130_9FUSO Unreviewed; 1262 AA.
AC U2T130;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:ERK68432.1};
GN ORFNames=HMPREF1984_00642 {ECO:0000313|EMBL:ERK68432.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK68432.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK68432.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK68432.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERK68432.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWVR01000017; ERK68432.1; -; Genomic_DNA.
DR RefSeq; WP_021767805.1; NZ_KI272867.1.
DR AlphaFoldDB; U2T130; -.
DR STRING; 1321779.HMPREF1984_00642; -.
DR PATRIC; fig|1321779.3.peg.624; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_003100_2_0_0; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000016640; 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 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:UP000016640}.
FT DOMAIN 183..231
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 446..596
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1103
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1262 AA; 141663 MW; 1BAA434E2C4F9532 CRC64;
MNYRIFVEKK EDFRVEAQNL MNDLRENVGI ESLDFLRILN IYDVFNLSKE ELEKMEKIVF
SEVNVDKVYN SLEEVFSAVE NKENKHFAVE FIPGQYDQRA DSAVQCIDLL ADNENFNVKS
GKLIVLYGNI TPEELAKIKK YYINEVEMRE KNLNILEENP EQENTEKVPV YENFINKTSE
EIADMRNNLE LAMTANDLLF IQEYFKNEEK RNPTETEIRV LDTYWSDHCR HTTFETIIDD
VKIENEEYRD IIEKTLGEYV KSREYVHGEK LGKKPMTLMD LATVFGKEQR KKGELPDLEV
SDEINACSIY IDVPVKGKTE KWILQFKNET HNHPTEIEPF GGASTCIGGA IRDPLSGRTF
VYQAVRISGS GDPTEKLNDT LKGKLPQRVI TQKAAHGYSS YGNQIGLATT YVNEIYDEGY
KAKRLELGLV VGAAPAENII REKPEKGDVV ILLGGRTGRD GIGGATGSSK EHTTESSEKC
SAEVQKGNAV TERKIQRLFR NKEVTQLIKK CNDFGAGGVS VAIGELADGL EIDLDKVRVK
YVGLTGTELA ISESQERMAV VVAEENVGKF IKLAEEENLE AYKVAEVNDT GRLVMKYRNE
VIADISREFL NTNGAKSNIN IEIEKTGKLN LERKIDGADF KERFINNLKD LNVCSQRGLM
ETFDSSIGST TVLMPYGGKY QLTPADVSVQ KVSVENAETD VASMVGYGYN PFVAKQSTFH
GGAYAVIESI AKVVAAGGNY KNIRFTFQEY FERLGKDSKK WGRPLSALLG AFHIQKEFGL
PSIGGKDSMS GTFNDISVPP TLVSFAVSMT TAENVISPEF KKAGNNIYLV RTAYDENDLP
DLKELKKNFD FITENIKNKK IVSAAAIKNG GLSEAVAKMA FGNKLGANIK SDGIIGENEW
FKAEYGTFIV ETAEKFDYEN AVLLGNVITE EKIVIDNKFE INLDELIEEW EKPLEKIFPT
RKEIENCHLL PHCNGTKYKK SELIERENVI SSFSNSIAKP RVFIPVFPGT NCEYDLERAF
NREGGIAKIG VFNNLTHENI LNSIDGFVKE IENSQILMLP GGFSAGDEPD GSAKFMVAVL
KNGRVKEAID KLLKRDGLIL GICNGFQALI KSGLLPYGEV RELNEDSPTL TFNNINKHMS
KIVMTKIISN NSPWLMGMNE GDIHAIPMSH GEGRIVITEE EYKKLYKNNQ IATKYVDFEG
NSSMDSQFNP NGSYYAIEGM LAHKGRIFGK MAHSERTGKN LYKNIYGNKD QNIFKNGVKF
FL
//
