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 01-MAY-2013, entry version 55.
DE RecName: Full=Histidinol-phosphate aminotransferase;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase;
GN Name=hisC; 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 -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000155; ABC31977.1; -; Genomic_DNA.
DR RefSeq; YP_436402.1; NC_007645.1.
DR HSSP; Q9X0D0; 2F8J.
DR ProteinModelPortal; Q2SBJ7; -.
DR STRING; 349521.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; AMENPFP; -.
DR ProtClustDB; PRK04870; -.
DR BioCyc; HCHE349521:GHAL-5136-MONOMER; -.
DR UniPathway; UPA00031; UER00012.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:HAMAP.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA: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; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; FALSE_NEG.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT CHAIN 1 363 Histidinol-phosphate aminotransferase.
FT /FTId=PRO_0000319762.
FT MOD_RES 219 219 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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
//
