GenomeNet

Database: UniProt
Entry: F8EW37_ZYMMT
LinkDB: F8EW37_ZYMMT
Original site: F8EW37_ZYMMT 
ID   F8EW37_ZYMMT            Unreviewed;       222 AA.
AC   F8EW37;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_01018};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_01018};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_01018};
GN   OrderedLocusNames=Zymop_1557 {ECO:0000313|EMBL:AEI38447.1};
OS   Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS   10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=579138 {ECO:0000313|EMBL:AEI38447.1, ECO:0000313|Proteomes:UP000000491};
RN   [1] {ECO:0000313|EMBL:AEI38447.1, ECO:0000313|Proteomes:UP000000491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 /
RC   NCIMB 11200 / NRRL B-4491 / Barker I
RC   {ECO:0000313|Proteomes:UP000000491};
RX   PubMed=21742897; DOI=10.1128/JB.05273-11;
RA   Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA   Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT   "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT   lectotype strain ATCC 29192.";
RL   J. Bacteriol. 193:5049-5050(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, ECO:0000256|HAMAP-Rule:MF_01018}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01018};
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, ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000256|ARBA:ARBA00011496, ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC       HisZ. {ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC       subfamily. {ECO:0000256|ARBA:ARBA00009489, ECO:0000256|HAMAP-
CC       Rule:MF_01018}.
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; CP002865; AEI38447.1; -; Genomic_DNA.
DR   RefSeq; WP_013934835.1; NC_015709.1.
DR   AlphaFoldDB; F8EW37; -.
DR   STRING; 579138.Zymop_1557; -.
DR   KEGG; zmp:Zymop_1557; -.
DR   PATRIC; fig|579138.3.peg.1650; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_2_0_5; -.
DR   OMA; YVMMDYD; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000491; 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   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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   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.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01018};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01018};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01018}.
FT   DOMAIN          56..212
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
SQ   SEQUENCE   222 AA;  24451 MW;  EDB501EA7FAF84A0 CRC64;
     MTKPLVFAIP KGRILKEALP MLEAAGIIPE AAFLDKESRL LRFTTNRHDV EIIRVRAFDV
     ATFVAHGAAQ MGIVGSDVIE EFSYPELYAP VDLNIGHCRL SIAEPKRLAQ GDDPREWSHV
     RVATKYPHLT HRHFEARGVQ AECIKLNGAM EIAPALGLAG RIVDLVSSGR TLEENGLVEV
     EKIMPISARL IVNRAAFKMR AGDIAPLVEN FRRLVGVTDN AA
//
DBGET integrated database retrieval system