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 29-MAY-2013, entry version 51.
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; LWEQGII; -.
DR ProtClustDB; PRK00950; -.
DR BioCyc; UMET351160:GJT4-732-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; 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; PyrdxlP-dep_Trfase_major; 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
//
