GenomeNet

Database: UniProt
Entry: Q0W253
LinkDB: Q0W253
Original site: Q0W253 
ID   HIS8_UNCMA              Reviewed;         361 AA.
AC   Q0W253;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   19-FEB-2014, entry version 53.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; OrderedLocusNames=UNCMA_07130; ORFNames=RCIX2460;
OS   Uncultured methanogenic archaeon RC-I.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanocellales;
OC   Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the
RT   rice rhizosphere.";
RL   Science 313:370-372(2006).
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   -!- 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; AM114193; CAJ37540.1; -; Genomic_DNA.
DR   RefSeq; YP_686866.1; NC_009464.1.
DR   ProteinModelPortal; Q0W253; -.
DR   STRING; 351160.RCIX2460; -.
DR   EnsemblBacteria; CAJ37540; CAJ37540; RCIX2460.
DR   GeneID; 5143587; -.
DR   KEGG; rci:RCIX2460; -.
DR   eggNOG; COG0079; -.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; TRLIFIC; -.
DR   ProtClustDB; PRK00950; -.
DR   BioCyc; UMET351160:GJT4-732-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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    361       Histidinol-phosphate aminotransferase.
FT                                /FTId=PRO_0000319803.
FT   MOD_RES     221    221       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   361 AA;  39954 MW;  649CF009351ED241 CRC64;
     MIRARQSVQE IKEYVAGKNV EEVAASYGID EKSIIKLASN ESCLGASPLA IEAIRKAACD
     AHVYPSVDAI ELREALAMRH GVPVRNIVCG NGMDAVIETL LRAFLETGDE VVIPLPAFSY
     YENVTRFCGA TPKYCARRAD FSLDVDAVLK QVTDRTKFIF ITSPNNPTGN LTSLAEIRSV
     ANAVDGIVFV DEAYIDFSGG KTALELMKEC DNIVIGRTMS KAWGLAGMRI GYGFMPDWIF
     REYMKVATPF ALSRIAIAAA LAALKDEEHY NRTVETVKAE RQFLMENVPF KVYPSEANFV
     LIDTAPLTSK HVVTEAMKRG VILRDCASFR EMGDRYVRIT VGTREQNVRL VEVLAEIKGS
     R
//
DBGET integrated database retrieval system