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Database: UniProt/SWISS-PROT
Entry: HIS8_HAHCH
LinkDB: HIS8_HAHCH
Original site: HIS8_HAHCH 
ID   HIS8_HAHCH              Reviewed;         363 AA.
AC   Q2SBJ7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   26-NOV-2014, entry version 64.
DE   RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023};
GN   OrderedLocusNames=HCH_05304;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
CC   -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC       (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC       {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR   EMBL; CP000155; ABC31977.1; -; Genomic_DNA.
DR   RefSeq; YP_436402.1; NC_007645.1.
DR   ProteinModelPortal; Q2SBJ7; -.
DR   STRING; 349521.HCH_05304; -.
DR   EnsemblBacteria; ABC31977; ABC31977; HCH_05304.
DR   GeneID; 3842018; -.
DR   KEGG; hch:HCH_05304; -.
DR   PATRIC; 22090960; VBIHahChe29232_4831.
DR   eggNOG; COG0079; -.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; EDCLRIT; -.
DR   OrthoDB; EOG6P5ZBR; -.
DR   BioCyc; HCHE349521:GHAL-5111-MONOMER; -.
DR   UniPathway; UPA00031; UER00012.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN         1    363       Histidinol-phosphate aminotransferase.
FT                                /FTId=PRO_0000319762.
FT   MOD_RES     219    219       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01023}.
SQ   SEQUENCE   363 AA;  39773 MW;  84D52E699A0FF8D7 CRC64;
     MSVKDRILQW VRPEVQALSA YHVADASGLI KLDAMENPFD FPAALKAELG VDLRDAAINR
     YPDPDAGAIR TALRELYSLP ASADMLFGNG SDEIIQILAM AVAGPGRTIL SVEPSFVMYK
     MIATFIGAEY VGVPLNDDFQ IDAQTTLDAI KRHQPALVFI AQPNNPTGNL FDDETLRQIV
     AASPGLVVID EAYTAFTNAD YMSWVSEYDN VVVMRTFSKV GLAGLRFGML FGAQEWIEQL
     NKVRLPYNIN CLTQNAVLTA IRHFPEFVKQ TEALREQRSW LSAQLDGVAG VTVYPSEANF
     ILVRVDLPAK SVFSEMKRRG VLIKLLDGGH PKLAGCLRLT VGSHEENEAM LKALSGALAA
     VRG
//
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