HIS1_ALKHC
ID HIS1_ALKHC Reviewed; 212 AA.
AC Q9K6Z1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=hisG; OrderedLocusNames=BH3583;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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 (By
CC similarity). {ECO:0000250}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000004; BAB07302.1; -; Genomic_DNA.
DR PIR; G84097; G84097.
DR RefSeq; WP_010899711.1; NC_002570.2.
DR AlphaFoldDB; Q9K6Z1; -.
DR SMR; Q9K6Z1; -.
DR STRING; 272558.10176207; -.
DR EnsemblBacteria; BAB07302; BAB07302; BAB07302.
DR KEGG; bha:BH3583; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_9; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 1419568at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13595; PBP2_HisGs; 1.
DR HAMAP; MF_01018; HisG_Short; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW Histidine biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..212
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151897"
SQ SEQUENCE 212 AA; 23807 MW; ED07BA42B2948F46 CRC64;
MSMLTVAMPK GRIFDEAVGL LRKAGYNLPA EFEASRKLIV DVPEENMRFI LAKPMDVPTY
VEHGVADVGV AGKDVMLEEE RDVYEVLDLK ISECYLAVAG LPNYEKKHDL NPKVASKYPH
LATRYFKEQG EQVEIIKLNG SIELAPLIGL ADRIVDIVST GRTLRENGLV ELEKMMTITS
RLIVNPVSYR MKDERIDEMV ERLLQVVEGD GA
