(data stored in SCRATCH zone)

SWISSPROT: D7A0V6_STAND

ID   D7A0V6_STAND            Unreviewed;       430 AA.
AC   D7A0V6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 65.
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_0129 {ECO:0000313|EMBL:ADH87466.1};
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:ADH87466.1, 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:ADH87466.1, 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; ADH87466.1; -; Genomic_DNA.
DR   RefSeq; WP_013164971.1; NC_014217.1.
DR   STRING; 639283.Snov_0129; -.
DR   EnsemblBacteria; ADH87466; ADH87466; Snov_0129.
DR   KEGG; sno:Snov_0129; -.
DR   eggNOG; ENOG4105CEK; Bacteria.
DR   eggNOG; COG0141; LUCA.
DR   HOGENOM; HOG000243914; -.
DR   KO; K00013; -.
DR   OMA; QAEHDPM; -.
DR   OrthoDB; 935289at2; -.
DR   BioCyc; SNOV639283:G1GLM-130-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; D7A0V6.
DR   SWISS-2DPAGE; D7A0V6.
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:ADH87466.1};
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    327    327       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   ACT_SITE    328    328       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   METAL       259    259       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       262    262       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       361    361       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       420    420       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   BINDING     130    130       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     191    191       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     214    214       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     237    237       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     259    259       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     262    262       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     328    328       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     361    361       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     415    415       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     420    420       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
SQ   SEQUENCE   430 AA;  45114 MW;  0B2FF8534AEC4741 CRC64;
     MPLRLDTASP EFKARFTAFL GTKREVSQDV AQAVARIIDD VRARGDDALI DFSRQFDRVD
     LGALGIRVTD TEIDAAEKAA DPAAREALAF AHERIRSHHQ RQLPESGRYV DAAGVELGHR
     WTAVDAVGLY VPGGTAAYPS SVLMNAVPAK VAGVKRVVMV VPAPDGQINP LVLAAAKLAG
     VDEVYRVGGA QAVAALAYGT QTIAPVAKIV GPGNAYVAAA KRHVFGTVGI DMVAGPSEVL
     VIADGAQNPD WIAADLLAQA EHDTAAQSIL MTDDAALADA VVYAVERQLT MLPRRDIAAA
     SWAEFGAVIK LKSLDEAPAL ADRIAPEHLE IMAADAEALA ERIHHAGAIF LGAHTPEAIG
     DYVGGSNHVL PTARSARFSS GLSVLDFMKR TSILKCGPEQ LRALGPAAIA LGEAEGLSAH
     ARSVAIRLNL
//

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