GenomeNet

Database: UniProt
Entry: A0A0M6XTK6_9RHOB
LinkDB: A0A0M6XTK6_9RHOB
Original site: A0A0M6XTK6_9RHOB 
ID   A0A0M6XTK6_9RHOB        Unreviewed;       227 AA.
AC   A0A0M6XTK6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN   Name=hisG {ECO:0000313|EMBL:CTQ33515.1};
GN   ORFNames=JAN5088_02297 {ECO:0000313|EMBL:CTQ33515.1};
OS   Jannaschia rubra.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ33515.1, ECO:0000313|Proteomes:UP000048908};
RN   [1] {ECO:0000313|EMBL:CTQ33515.1, ECO:0000313|Proteomes:UP000048908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ33515.1,
RC   ECO:0000313|Proteomes:UP000048908};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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   ---------------------------------------------------------------------------
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; CXPG01000020; CTQ33515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M6XTK6; -.
DR   STRING; 282197.SAMN04488517_102344; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000048908; 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   CDD; cd13593; PBP2_HisGL3; 1.
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   NCBIfam; TIGR00070; hisG; 1.
DR   PANTHER; PTHR21403:SF8; 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:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:CTQ33515.1};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000048908};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CTQ33515.1}.
FT   DOMAIN          53..224
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
SQ   SEQUENCE   227 AA;  24986 MW;  EA979F4E6DA14D71 CRC64;
     MLRLGVPSKG RLMDKTFDWF GKRGLTLTRS GSDREYAGHV EGADIALVML SAGEIPRELA
     AGRIHLGVTG SDLVRERLTR WDTRVKALAP MGFGHADLIL AVPKVWIDVD TLDDLDAACA
     QFRATHGHRL RIATKYHRLV RDFLRQNGVA DYQLVDSQGA TEGTVLNHTA EAIADITSTG
     ETMRANHLKV LDDGLIHASQ ATLFRALDAP WDKAAKAVLE DLRERLA
//
DBGET integrated database retrieval system