(data stored in SCRATCH zone)

SWISSPROT: D7A138_STAND

ID   D7A138_STAND            Unreviewed;       438 AA.
AC   D7A138;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
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=Snov_0212 {ECO:0000313|EMBL:ADH87548.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87548.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87548.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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:
CC       Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2
CC         NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01024,
CC         ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS01118474};
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; CP002026; ADH87548.1; -; Genomic_DNA.
DR   RefSeq; WP_013165053.1; NC_014217.1.
DR   STRING; 639283.Snov_0212; -.
DR   EnsemblBacteria; ADH87548; ADH87548; Snov_0212.
DR   KEGG; sno:Snov_0212; -.
DR   eggNOG; ENOG4105CEK; Bacteria.
DR   eggNOG; COG0141; LUCA.
DR   HOGENOM; HOG000243914; -.
DR   KO; K15509; -.
DR   OMA; MTDRDDW; -.
DR   OrthoDB; 935289at2; -.
DR   BioCyc; SNOV639283:G1GLM-212-MONOMER; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000006633; 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; D7A138.
DR   SWISS-2DPAGE; D7A138.
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:UP000006633};
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:ADH87548.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-
KW   4, ECO:0000256|SAAS:SAAS00781803}.
FT   ACT_SITE    318    318       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   ACT_SITE    319    319       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   METAL       250    250       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       253    253       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       352    352       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       412    412       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   BINDING     121    121       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     182    182       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     205    205       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     228    228       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     250    250       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     253    253       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     319    319       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     352    352       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     407    407       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     412    412       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
SQ   SEQUENCE   438 AA;  47007 MW;  D8A6753BDB84CC56 CRC64;
     MARHLKTARS VEERADADAQ VRATVETILA EIEAGGDAAV RAYSERFDTW SPASFRLSER
     EIEKALSQVS KSDLDDIRFA QAQVRNFAEK QRACLTDLEV ETLPGVILGH KNVPVERVGC
     YVPGGKYPMV ASAHMSVVTA KVAGVKSVVA AAPPFRNGPH PAIVAAMHFA GADEILVLGG
     VQAVAAMALG TETIAPVDML VGPGNAYVAE AKRQLYGRVG IDLFAGPTET LVIADETVDA
     EICATDLLGQ AEHGPTSPAI LLTNSEKLAR ETMAEVERLL AILPTGEIAS VAWRDFGEVI
     VCDDVEEMVR EADRIASEHV QVMTADPDYF LANMRNYGAL FLGPRTNVAY GDKVIGTNHT
     LPTRRAARYT GGLWVGKFLK TCTYQKVTSD AASAEVGEYC SRLCVLEGFL GHAEQANVRV
     RRYGGGNVDY ATAARRAG
//

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