ID A0A166CUR3_9EURY Unreviewed; 328 AA.
AC A0A166CUR3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN Name=hisG_1 {ECO:0000313|EMBL:KZX14886.1};
GN ORFNames=MBCUR_03390 {ECO:0000313|EMBL:KZX14886.1};
OS Methanobrevibacter curvatus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=49547 {ECO:0000313|EMBL:KZX14886.1, ECO:0000313|Proteomes:UP000077245};
RN [1] {ECO:0000313|EMBL:KZX14886.1, ECO:0000313|Proteomes:UP000077245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11111 {ECO:0000313|EMBL:KZX14886.1,
RC ECO:0000313|Proteomes:UP000077245};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter curvatus DSM 11111.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial
CC role in the pathway because the rate of histidine biosynthesis seems to
CC be controlled primarily by regulation of HisG enzymatic activity.
CC {ECO:0000256|ARBA:ARBA00024861}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:73183; EC=2.4.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000915};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC {ECO:0000256|ARBA:ARBA00004667}.
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:KZX14886.1}.
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DR EMBL; LWMV01000062; KZX14886.1; -; Genomic_DNA.
DR RefSeq; WP_067089416.1; NZ_LWMV01000062.1.
DR AlphaFoldDB; A0A166CUR3; -.
DR STRING; 49547.MBCUR_03390; -.
DR PATRIC; fig|49547.3.peg.358; -.
DR OrthoDB; 33116at2157; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000077245; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR PANTHER; PTHR21403:SF10; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glycosyltransferase {ECO:0000313|EMBL:KZX14886.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Reference proteome {ECO:0000313|Proteomes:UP000077245};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZX14886.1}.
FT DOMAIN 58..245
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 328 AA; 36687 MW; 232D42DF538F74E5 CRC64;
MAKIILGLPK GSLNNVNRGN TYQLFVDAGY EVKGYEPGNE SYEIDITNDN DIKSYLTRPQ
STPVELNRGM VDIAIVGEDW VKEESVVNKN TIEKIGDLNY GETRLIVAVP QESEYDNLTG
FFRKNKDRKT PILCFTEYPN LTRQHIMNNE GYKEIFGDKV PFVQVRSLTD GDNEKIQIIN
SDGATEVYIA KGADLVVDNT QTGSSLKKAG LKELETIMHS SAGLYAGPSC VGEKIEKAKM
IFEQLLGATT GRSYFDVKFN VLNDLAIKAS EFLITNKYCS DEPTINQGTE YSQINVLISK
KLFPEMLNGI KQFNASAIVR NNVKQYIK
//
