(data stored in ACNUC7421 zone)

HOGENOM: HALBP_1_PE10

ID   HALBP_1_PE10                         STANDARD;      PRT;   281 AA.
AC   HALBP_1_PE10; E4NQZ7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP phosphoribosyltransferase; Short=ATP-PRT;
DE   Short=ATP-PRTase; EC=2.4.2 17; (HALBP_1.PE10).
GN   Name=hisG; OrderedLocusNames=Hbor_00100;
OS   HALOGEOMETRICUM BORINQUENSE DSM 11551.
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Halobacteriaceae;
OC   Halogeometricum.
OX   NCBI_TaxID=469382;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HALBP_1.PE10.
CC       Halogeometricum borinquense DSM 11551 chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E4NQZ7_HALBP
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 1-(5-phospho-D-ribosyl)-ATP + diphosphate =
CC       ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Feedback inhibited by histidine (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Long subfamily.
CC   -!- GENE_FAMILY: HOG000223247 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E4NQZ7; -.
DR   EMBL; CP001690; ADQ65623.1; -; Genomic_DNA.
DR   RefSeq; YP_004035062.1; NC_014729.1.
DR   GeneID; 9991830; -.
DR   GenomeReviews; CP001690_GR; Hbor_00100.
DR   KEGG; hbo:Hbor_00100; -.
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:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00079; HisG_Long; 1; -.
DR   InterPro; IPR001348; ATP_PRibTrfase.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR020621; ATP_PRibTrfase_subgr.
DR   InterPro; IPR013115; HisG_C.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   Gene3D; G3DSA:3.30.70.120; PII_glnB; 1.
DR   PANTHER; PTHR21403; ATP_phspho_trans; 1.
DR   Pfam; PF01634; HisG; 1.
DR   Pfam; PF08029; HisG_C; 1.
DR   SUPFAM; SSF54913; N-reg_PII-like_a/b; 1.
DR   TIGRFAMs; TIGR00070; HisG; 1.
DR   TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR   HOGENOMDNA; HALBP_1.PE10; -.
KW   ATP phosphoribosyltransferase (homohexameric);
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
SQ   SEQUENCE   281 AA;  UNKNOWN MW;  UNKNOWN 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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