ID G0QB28_NANSJ Unreviewed; 213 AA.
AC G0QB28;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN ORFNames=J07AB56_13180 {ECO:0000313|EMBL:EGQ40588.1};
OS Nanosalinarum sp. (strain J07AB56).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Nanosalinarum.
OX NCBI_TaxID=889962 {ECO:0000313|EMBL:EGQ40588.1, ECO:0000313|Proteomes:UP000009382};
RN [1] {ECO:0000313|EMBL:EGQ40588.1, ECO:0000313|Proteomes:UP000009382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C., Emerson J.B.,
RA Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "De novo metagenomic assembly reveals abundant novel major lineage of
RT Archaea in hypersaline microbial communities.";
RL ISME J. 0:0-0(2011).
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}.
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DR EMBL; GL982569; EGQ40588.1; -; Genomic_DNA.
DR AlphaFoldDB; G0QB28; -.
DR HOGENOM; CLU_1292056_0_0_2; -.
DR Proteomes; UP000009382; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
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:EGQ40588.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Reference proteome {ECO:0000313|Proteomes:UP000009382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGQ40588.1}.
FT DOMAIN 59..197
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 213 AA; 23510 MW; F8ACA6C81D32D82B CRC64;
MSESSPKPEV GLAKNDEMLP GVTRYLEQLG VNTGDFPEEE RGRSYTVDRP EARYSFLNAS
DVAGCYMDGI LDAGMTGSDW AFEWALRKGK TLQDVKWMPA YILDGEGGKE SFGDVRRVLA
SPDGNLSQEP YVAAEKPDSA RFFLEDSYPG SDVKAINGSS EVFPKYDGVD AYFGIVESGN
TMKQNGMEPV EHYEKSTGVW LGQNPWDLFG TNL
//