ID R4LZ22_MYCTX Unreviewed; 251 AA.
AC R4LZ22;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN Name=hisG {ECO:0000313|EMBL:AGL23745.1};
GN ORFNames=I917_14900 {ECO:0000313|EMBL:AGL23745.1};
OS Mycobacterium tuberculosis str. Haarlem/NITR202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1304279 {ECO:0000313|EMBL:AGL23745.1, ECO:0000313|Proteomes:UP000013563};
RN [1] {ECO:0000313|EMBL:AGL23745.1, ECO:0000313|Proteomes:UP000013563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Haarlem/NITR202 {ECO:0000313|EMBL:AGL23745.1,
RC ECO:0000313|Proteomes:UP000013563};
RX PubMed=23788533;
RA Narayanan S., Deshpande U.;
RT "Whole-Genome Sequences of Four Clinical Isolates of Mycobacterium
RT tuberculosis from Tamil Nadu, South India.";
RL Genome Announc. 1:e00186-13(2013).
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; CP004886; AGL23745.1; -; Genomic_DNA.
DR KEGG; mtuh:I917_14900; -.
DR PATRIC; fig|1304279.3.peg.2186; -.
DR HOGENOM; CLU_038115_1_1_11; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000013563; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.120; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR NCBIfam; TIGR00070; hisG; 1.
DR NCBIfam; TIGR03455; HisG_C-term; 1.
DR PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; GlnB-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:AGL23745.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGL23745.1}.
FT DOMAIN 16..171
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 177..247
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
SQ SEQUENCE 251 AA; 26899 MW; 3AA7F4991D5D0915 CRC64;
MTVIDPVNNV EFFFLRPKDI AIYVGSGELD FGITGRDLVC DSGAQVRERL ALGFGSSSFR
YAAPAGRNWT TADLAGMRIA TAYPNLVRKD LATKGIEATV IRLDGAVEXS VQLGVADAIA
DVVGSGRTLS QHDLVAFGEP LCDSEAVLIE RAGTDGQDQT EARDQLVARV QGVVFGQQYL
MLDYDCPRSA LKKATAITPG LESPTIAPLA DPDWVAIRAL VPRRDVNGIM DELAAIGAKA
ILASDIRFCR F
//