(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BII6_GEOS0

ID   A0A0F6BII6_GEOS0        Unreviewed;       206 AA.
AC   A0A0F6BII6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01018, ECO:0000256|SAAS:SAAS00008790};
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|HAMAP-Rule:MF_01018, ECO:0000256|SAAS:SAAS00046302};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_01018};
GN   OrderedLocusNames=GY4MC1_0396 {ECO:0000313|EMBL:ADP73237.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73237.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73237.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73237.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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
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_01018,
CC       ECO:0000256|SAAS:SAAS00046314}.
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_01018,
CC         ECO:0000256|SAAS:SAAS01121154};
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_01018, ECO:0000256|SAAS:SAAS00046315}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_01018, ECO:0000256|SAAS:SAAS00008816}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01018,
CC       ECO:0000256|SAAS:SAAS00046328}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced
CC       by HisZ. {ECO:0000256|HAMAP-Rule:MF_01018}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Short subfamily. {ECO:0000256|HAMAP-Rule:MF_01018,
CC       ECO:0000256|SAAS:SAAS00586253}.
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DR   EMBL; CP002293; ADP73237.1; -; Genomic_DNA.
DR   RefSeq; WP_003248066.1; NC_014650.1.
DR   EnsemblBacteria; ADP73237; ADP73237; GY4MC1_0396.
DR   GeneID; 29236946; -.
DR   KEGG; gmc:GY4MC1_0396; -.
DR   KO; K00765; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; 1419568at2; -.
DR   BioCyc; GSP581103:G1GOQ-441-MONOMER; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002034; 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;
DR   PRODOM; A0A0F6BII6.
DR   SWISS-2DPAGE; A0A0F6BII6.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046310};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046309};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046320};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046307, ECO:0000313|EMBL:ADP73237.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046316};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046318};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01018,
KW   ECO:0000256|SAAS:SAAS00046311, ECO:0000313|EMBL:ADP73237.1}.
FT   DOMAIN       51    201       HisG. {ECO:0000259|Pfam:PF01634}.
SQ   SEQUENCE   206 AA;  22966 MW;  E7175D59DF9B2FCE CRC64;
     MLTIAMPKGR IFAEALELLQ KAGYTLPAEF AESRKLMMEV PEENMRFILA KPMDVVTYVE
     HGVADLGIAG KDVMMEEERD VYELLDLKIS KCHLAVAGLP NGRMPQIAPR VATKYPNIAS
     SYFREQGEQV EIIRLNGSIE LAPLIGLADR IVDIVSTGRT LKENGLVELE KIADVTSRLI
     VNPVSYRIKD EEVDVLVCRL SEVIPQ
//

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