ID B5YHM2_THEYD Unreviewed; 423 AA.
AC B5YHM2;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 01-MAY-2013, entry version 39.
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=hisD; OrderedLocusNames=THEYE_A1817;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 /
OS YP87).
OC Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae;
OC Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii
RT strain ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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.
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DR EMBL; CP001147; ACI21602.1; -; Genomic_DNA.
DR RefSeq; YP_002249608.1; NC_011296.1.
DR ProteinModelPortal; B5YHM2; -.
DR STRING; 289376.THEYE_A1817; -.
DR EnsemblBacteria; ACI21602; ACI21602; THEYE_A1817.
DR GeneID; 6941631; -.
DR KEGG; tye:THEYE_A1817; -.
DR PATRIC; 23910661; VBITheYel104483_1773.
DR eggNOG; COG0141; -.
DR HOGENOM; HOG000243914; -.
DR KO; K00013; -.
DR OMA; PTYGYSR; -.
DR UniPathway; UPA00031; UER00014.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:HAMAP.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
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 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT ACT_SITE 320 320 Proton acceptor (By similarity).
FT ACT_SITE 321 321 Proton acceptor (By similarity).
FT METAL 252 252 Zinc (By similarity).
FT METAL 255 255 Zinc (By similarity).
FT METAL 354 354 Zinc (By similarity).
FT METAL 413 413 Zinc (By similarity).
FT BINDING 123 123 NAD (By similarity).
FT BINDING 184 184 NAD (By similarity).
FT BINDING 207 207 NAD (By similarity).
FT BINDING 230 230 Substrate (By similarity).
FT BINDING 252 252 Substrate (By similarity).
FT BINDING 255 255 Substrate (By similarity).
FT BINDING 321 321 Substrate (By similarity).
FT BINDING 354 354 Substrate (By similarity).
FT BINDING 408 408 Substrate (By similarity).
FT BINDING 413 413 Substrate (By similarity).
SQ SEQUENCE 423 AA; 46343 MW; ABDD40ABCBA42097 CRC64;
MQIIKDKKIF EKFVKKLQKR SFSEPKIEDS VRKILNDIKK SGDKALARYT KLFDKHSLPL
KIGKKEIEKK AKDISKDVFN ALIFAEERIR KFHEKQLEKS WQYQEGDIIL GQIIRPLERV
GAYVPGGKAS YPSTVLMNII PAQVAGVKEI AVCVPTPNGE LNPIVCAALS ILGIKEVYRI
GGAQAIAAMA YGTETIKKVD KIVGPGNIYV ATAKKLVFGE VDIDMIAGPS EILIIADNSA
NPAFVAADML SQAEHDEMAC SILVTNSEQL VNSVKKEITR QLKKLPKASI AKESLKNFGA
IIIVKSLQEA CNIANTIAPE HLEVMTENPE KLLPLLKNAG AIFLGQFTPE PIGDYVAGPN
HTLPTSGTAR FFSPLGVYDF VKKSSLIKVG ENGFNKLAPY VEVLATLEGL HAHANTVKVR
KTT
//
