(data stored in ACNUC7421 zone)

SWISSPROT: E4NQZ7_HALBP

ID   E4NQZ7_HALBP            Unreviewed;       281 AA.
AC   E4NQZ7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   16-JAN-2019, entry version 55.
DE   RecName: Full=ATP phosphoribosyltransferase {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|HAMAP-Rule:MF_00079};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079,
GN   ECO:0000313|EMBL:ELY27841.1};
GN   OrderedLocusNames=Hbor_00100 {ECO:0000313|EMBL:ADQ65623.1};
GN   ORFNames=C499_08357 {ECO:0000313|EMBL:ELY27841.1};
OS   Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM
OS   10706 / PR3).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Halogeometricum.
OX   NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ65623.1, ECO:0000313|Proteomes:UP000006663};
RN   [1] {ECO:0000313|EMBL:ADQ65623.1, ECO:0000313|Proteomes:UP000006663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / PR3
RC   {ECO:0000313|Proteomes:UP000006663}, and PR 3
RC   {ECO:0000313|EMBL:ADQ65623.1};
RX   PubMed=21304651; DOI=10.4056/sigs.23264;
RA   Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA   Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F.,
RA   Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Anderson I., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Halogeometricum borinquense type strain
RT   (PR3).";
RL   Stand. Genomic Sci. 1:150-159(2009).
RN   [2] {ECO:0000313|Proteomes:UP000011585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11551 {ECO:0000313|Proteomes:UP000011585};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
RA   Darling A., Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ELY27841.1, ECO:0000313|Proteomes:UP000011585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY27841.1,
RC   ECO:0000313|Proteomes:UP000011585};
RX   PubMed=25393412;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
RA   Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea
RT   reveals strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC       diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a
CC       crucial role in the pathway because the rate of histidine
CC       biosynthesis seems to be controlled primarily by regulation of
CC       HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + ATP;
CC         Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00079};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Long subfamily. {ECO:0000256|HAMAP-Rule:MF_00079}.
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DR   EMBL; CP001690; ADQ65623.1; -; Genomic_DNA.
DR   EMBL; AOHT01000030; ELY27841.1; -; Genomic_DNA.
DR   RefSeq; WP_006054988.1; NZ_AOHT01000030.1.
DR   STRING; 469382.Hbor_00100; -.
DR   EnsemblBacteria; ADQ65623; ADQ65623; Hbor_00100.
DR   EnsemblBacteria; ELY27841; ELY27841; C499_08357.
DR   GeneID; 9991830; -.
DR   KEGG; hbo:Hbor_00100; -.
DR   PATRIC; fig|469382.19.peg.1640; -.
DR   eggNOG; arCOG02208; Archaea.
DR   eggNOG; COG0040; LUCA.
DR   HOGENOM; HOG000223247; -.
DR   KO; K00765; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; 56745at2157; -.
DR   BioCyc; HBOR469382:G1GPB-10-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000006663; Chromosome.
DR   Proteomes; UP000011585; Unassembled WGS sequence.
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   Gene3D; 3.30.70.120; -; 1.
DR   HAMAP; MF_00079; HisG_Long; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
DR   InterPro; IPR013115; HisG_C.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   PANTHER; PTHR21403; PTHR21403; 1.
DR   Pfam; PF01634; HisG; 1.
DR   Pfam; PF08029; HisG_C; 1.
DR   SUPFAM; SSF54913; SSF54913; 1.
DR   TIGRFAMs; TIGR00070; hisG; 1.
DR   TIGRFAMs; TIGR03455; HisG_C-term; 1.
PE   3: Inferred from homology;
DR   PRODOM; E4NQZ7.
DR   SWISS-2DPAGE; E4NQZ7.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006663,
KW   ECO:0000313|Proteomes:UP000011585};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000313|EMBL:ADQ65623.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079};
KW   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:UP000006663};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000313|EMBL:ADQ65623.1}.
FT   DOMAIN       49    201       HisG. {ECO:0000259|Pfam:PF01634}.
FT   DOMAIN      206    278       HisG_C. {ECO:0000259|Pfam:PF08029}.
SQ   SEQUENCE   281 AA;  30395 MW;  0D2E669F5B726FE5 CRC64;
     MRIAVPNKGR LHDPSVELLE RAGLHIQSGA DRKLYADTVD PDVTVLFARA ADIPEYVRDG
     AAAVGITGLD QMRESGHDLE ELVDLQFGSC RLVLAAPEDG DIESVEDVAG KIVATEFPTI
     ARNYFDEQGV EADVVEVSGA TELTPHVEMA DAIIDITSTG TTLRVNRLAI VDEVLSSSVR
     LFARPDVVDD PKVDQLVTAF QSVIAAEDKR YVMMNVPQER LDDVREVLPG LGGPTVMDVA
     GDDMVAVHAV VDERHVFEVV NDLKSVGASG ILVTEIERLV E
//

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