(data stored in ACNUC7421 zone)

SWISSPROT: D3F4Y6_CONWI

ID   D3F4Y6_CONWI            Unreviewed;       444 AA.
AC   D3F4Y6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213};
DE            Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099};
DE            EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024};
GN   OrderedLocusNames=Cwoe_0128 {ECO:0000313|EMBL:ADB48564.1};
OS   Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 /
OS   ID131577).
OC   Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB48564.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) 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.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|SAAS:SAAS00728939}.
CC   -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine
CC       + 2 NADH. {ECO:0000256|HAMAP-Rule:MF_01024,
CC       ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729200}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-4};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-4};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|SAAS:SAAS00729141}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|RuleBase:RU004175, ECO:0000256|SAAS:SAAS00827949}.
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DR   EMBL; CP001854; ADB48564.1; -; Genomic_DNA.
DR   RefSeq; WP_012931617.1; NC_013739.1.
DR   ProteinModelPortal; D3F4Y6; -.
DR   STRING; 469383.Cwoe_0128; -.
DR   EnsemblBacteria; ADB48564; ADB48564; Cwoe_0128.
DR   KEGG; cwo:Cwoe_0128; -.
DR   eggNOG; ENOG4105CEK; Bacteria.
DR   eggNOG; COG0141; LUCA.
DR   HOGENOM; HOG000243914; -.
DR   KO; K15509; -.
DR   OMA; MTDRDDW; -.
DR   OrthoDB; POG091H03YX; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000008229; Chromosome.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd06572; Histidinol_dh; 1.
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; SSF53720; 1.
DR   TIGRFAMs; TIGR00069; hisD; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3F4Y6.
DR   SWISS-2DPAGE; D3F4Y6.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729217};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008229};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728911};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRSR:PIRSR000099-4, ECO:0000256|SAAS:SAAS00781816};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
KW   ECO:0000256|PIRSR:PIRSR000099-2, ECO:0000256|SAAS:SAAS00751613};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00751612,
KW   ECO:0000313|EMBL:ADB48564.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-
KW   4, ECO:0000256|SAAS:SAAS00781803}.
FT   ACT_SITE    335    335       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   ACT_SITE    336    336       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   METAL       267    267       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       270    270       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       369    369       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       428    428       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   BINDING     138    138       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     199    199       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     222    222       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     245    245       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     267    267       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     270    270       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     336    336       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     369    369       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     423    423       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     428    428       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
SQ   SEQUENCE   444 AA;  46946 MW;  A0F705E9C6638328 CRC64;
     MAEVLKAARD GWTGARTRSG RATSEGGDRA NGASDPAVVA TVAEIIGAVR ERGDAAVREL
     SARFDRWEPE SFRLTTEQID ACVAQVSEQA LADLRWCQEQ VRAFALAQRA SLHDVEVETQ
     PGVRLGHRHV PIARVGAYIP GGRYPMIASA AMSILTAKAA GVEHVIACTP PLDGAPPALT
     VAAMQLAGAD EIHVLGGVQA VAAMAVGTET IERVDFLAGP GNAYVAEAKR QLFGEVGIDL
     FAGPTEILVV ADETADPEIV AADLLGQAEH GLTSPAALIA TDAGLARAAL AEIERQLQTL
     PTADVAGPAW RDYGEVHLVG DREEAAALAD AFAYEHVEIL TAEPRWFLDT LRQYGALFLG
     EGTTVAYGDK AIGTNHVLPT AGAARYTGGL WVGKFLKTVT YQECDPAASA RIGEICARQC
     RLEHFEGHAR SCDVRVRKYA GALV
//

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