(data stored in SCRATCH zone)

SWISSPROT: D1YWF4_METPS

ID   D1YWF4_METPS            Unreviewed;       423 AA.
AC   D1YWF4;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099};
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};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024,
GN   ECO:0000313|EMBL:BAI60776.1};
GN   OrderedLocusNames=MCP_0704 {ECO:0000313|EMBL:BAI60776.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60776.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC         Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC         ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01024,
CC         ECO:0000256|PIRSR:PIRSR000099-4};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01024,
CC       ECO:0000256|PIRSR:PIRSR000099-4};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|RuleBase:RU004175}.
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DR   EMBL; AP011532; BAI60776.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0704; -.
DR   EnsemblBacteria; BAI60776; BAI60776; MCP_0704.
DR   KEGG; mpd:MCP_0704; -.
DR   PATRIC; fig|304371.9.peg.728; -.
DR   eggNOG; arCOG04352; Archaea.
DR   eggNOG; COG0141; LUCA.
DR   HOGENOM; HOG000243914; -.
DR   KO; K00013; -.
DR   OMA; QAEHDPM; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR21256; PTHR21256; 1.
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; D1YWF4.
DR   SWISS-2DPAGE; D1YWF4.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRSR:PIRSR000099-4};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
KW   ECO:0000256|PIRSR:PIRSR000099-2};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-4}.
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   METAL           256
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   METAL           259
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   METAL           355
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   METAL           414
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         126
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         188
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         211
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         234
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         256
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         259
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         322
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         355
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         409
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         414
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
SQ   SEQUENCE   423 AA;  45690 MW;  61BCEBFFECC95BC4 CRC64;
     MIKQLYGVDD AALDEVFKRR TSISSVMDTA KKVADEVREG GDAAVRKYTK QFDGVDLRDL
     EVTDDEMYNA VELIDYETIG HLEKAIDNIE AFHALQRPSG DMWLTEISPG IRLGQKFTPL
     ERIGAYVPGG TGSYPSTALM LIVPAQVAGV SEIIACTPPR KDGTIHPLTL TALDMAGADR
     IFKVGGVQAI AAMAYGTQSI PKVEKIVGPG NIYVTAAKMY VRDAAEIDMP AGPSEIVVIA
     DDTAIPSFIA SDMIAQAEHD VNAMSILLTP SEMLAESVEL EIERQKENAP RRQIIDKAGM
     GIYVLDDLDA AVEVCNRIAP EHVEIMVRDP MSTLNKVRNA GTVYVGDYAP VAAGDYASGA
     NHVLPTGGYA KVFSGMNTMQ FIKTTSVQVI EKGGLEGIKD TITALAEIEG FDAHARSVYK
     RFE
//

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