GenomeNet

Database: UniProt
Entry: D5UPK5_TSUPD
LinkDB: D5UPK5_TSUPD
Original site: D5UPK5_TSUPD 
ID   D5UPK5_TSUPD            Unreviewed;       281 AA.
AC   D5UPK5;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_00079};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_00079};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079};
GN   OrderedLocusNames=Tpau_2150 {ECO:0000313|EMBL:ADG78761.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP
OS   100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040)
OS   (Corynebacterium paurometabolum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG78761.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC   KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Munk A.C., Brettin T., Detter J.C., Tapia R., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Jando M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG78761.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC   KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Tapia R.,
RA   Han C., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA   Yasawong M., Brambilla E.M., Rohde M., Sikorski J., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain (no.
RT   33).";
RL   Stand. Genomic Sci. 4:342-351(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_00079}.
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_00079};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00079};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC       {ECO:0000256|HAMAP-Rule:MF_00079}.
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_00079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC       subfamily. {ECO:0000256|ARBA:ARBA00007955, ECO:0000256|HAMAP-
CC       Rule:MF_00079}.
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; CP001966; ADG78761.1; -; Genomic_DNA.
DR   RefSeq; WP_013126783.1; NC_014158.1.
DR   AlphaFoldDB; D5UPK5; -.
DR   STRING; 521096.Tpau_2150; -.
DR   KEGG; tpr:Tpau_2150; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_1_1_11; -.
DR   OMA; YVMMDYD; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001213; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13591; PBP2_HisGL1; 1.
DR   Gene3D; 3.30.70.120; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   HAMAP; MF_00079; HisG_Long; 1.
DR   InterPro; IPR020621; ATP-PRT_HisG_long.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00079}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00079};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_00079}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00079}.
FT   DOMAIN          49..201
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
FT   DOMAIN          207..277
FT                   /note="Histidine biosynthesis HisG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08029"
SQ   SEQUENCE   281 AA;  30372 MW;  0BA07CEB1D65F2D9 CRC64;
     MLRVAVPNKG ALSEAAAAIL SEAGYRRRSD AKDLTVIDNA NEVEFFFLRP KDIALYVGSG
     ELDMGITGRD LALDSGAEFT ERLALGFGRS TFRYAGPAGI EWSVDDLDGK RVATSYPNLV
     RRDLAQRGIA ADVIRLDGAV EISIQLGVAD LIADVVESGR SLRQNNLVAF GESLCDSEGV
     LIERVGAESD RARDQLTARL KGVVFGRQYV MLDYDCPRTL LDGAIAVTPG LESPTVAPMA
     DEKWVAVRAM VLRKDANGVM DDLAELGAKA ILMTDIRSCR F
//
DBGET integrated database retrieval system