(data stored in ACNUC7421 zone)

HOGENOM: DESDG_1_PE1009

ID   DESDG_1_PE1009                       STANDARD;      PRT;   434 AA.
AC   DESDG_1_PE1009; Q313T7;
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=Histidinol dehydrogenase; Short=HDH; EC=1.1.1 23;
DE   (DESDG_1.PE1009).
GN   Name=hisD; OrderedLocusNames=Dde_1008;
OS   DESULFOVIBRIO ALASKENSIS G20.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=207559;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESDG_1.PE1009.
CC       Desulfovibrio desulfuricans subsp. desulfuricans str. G20 chromosome,
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:HISX_DESDG
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine
CC       + 2 NADH.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC   -!- GENE_FAMILY: HOG000243914 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q313T7; -.
DR   EMBL; CP000112; ABB37809.1; -; Genomic_DNA.
DR   RefSeq; YP_387504.1; NC_007519.1.
DR   ProteinModelPortal; Q313T7; -.
DR   STRING; Q313T7; -.
DR   GeneID; 3755510; -.
DR   GenomeReviews; CP000112_GR; Dde_1008.
DR   KEGG; dde:Dde_1008; -.
DR   NMPDR; fig|207559.3.peg.27; -.
DR   eggNOG; COG0141; -.
DR   OMA; IEAFHRQ; -.
DR   ProtClustDB; PRK00877; -.
DR   BioCyc; DDES207559:DDE_1008-MON; -.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01024; HisD; 1; -.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR022695; Histidinol_DH_monofunct.
DR   InterPro; IPR012131; Hstdl_DH.
DR   PANTHER; PTHR21256:SF2; Hstdl_DH_prok; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PIRSF; PIRSF000099; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   TIGRFAMs; TIGR00069; HisD; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
DR   HOGENOMDNA; DESDG_1.PE1009; -.
KW   Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
SQ   SEQUENCE   434 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPCRTLTYSS EADWQGIRDM LCGRENPENS VEPVVREIMD AIRSDGDAAL AGYTRRFDCP
     DFDPSSLRVA PDAIEKAARE IPRHDLQIIT EAADNIRHFH SAQKEEAWFI TRPDGTVLGQ
     MTRPVDSAGL YVPGGQGGNT PLISSLLMNA VPAQVAGVPR IAVTTPPRKD GTLNPYILAA
     AHVLGLDEIY CAGSAWAVAA LAYGTQTIAP VDFIAGPGNI FVTTAKRMLI GTVGIDMIAG
     PSEILIIADS QADAAHVAAD MLSQAEHDPL ASAILVTPSP QLAAAVHTEL EKQVTGLDRA
     DIARASLRDW SAIVVTPDLN SAVELSNKVA PEHLELLVQD TWGLLGSIRN AGAIFMGPHS
     PEPVGDYFAG PNHVLPTMGT ARFSSALSVQ SFCKKSSIIA ASQTFTQTNA AKIARLARLE
     GLEAHARSVE SRLS
//

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