(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BII7_GEOS0

ID   A0A0F6BII7_GEOS0        Unreviewed;       422 AA.
AC   A0A0F6BII7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 27.
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=GY4MC1_0397 {ECO:0000313|EMBL:ADP73238.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73238.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73238.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73238.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-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:
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; CP002293; ADP73238.1; -; Genomic_DNA.
DR   RefSeq; WP_013400003.1; NC_014650.1.
DR   EnsemblBacteria; ADP73238; ADP73238; GY4MC1_0397.
DR   GeneID; 29236945; -.
DR   KEGG; gmc:GY4MC1_0397; -.
DR   KO; K00013; -.
DR   OMA; QAEHDPM; -.
DR   OrthoDB; 935289at2; -.
DR   BioCyc; GSP581103:G1GOQ-442-MONOMER; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000002034; 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; A0A0F6BII7.
DR   SWISS-2DPAGE; A0A0F6BII7.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729217};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
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:ADP73238.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-
KW   4, ECO:0000256|SAAS:SAAS00781803}.
FT   COILED       54     81       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    319    319       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   ACT_SITE    320    320       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   METAL       251    251       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       254    254       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       353    353       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     183    183       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     206    206       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     229    229       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     251    251       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     254    254       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     320    320       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     353    353       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   422 AA;  45746 MW;  CE59974E06123293 CRC64;
     MKIERVKSRV SLRRTIESGT EEQRRAVLEI ISTVRARGDE ALKSYTEKFD GVRLDSLRVT
     NEEIEAAYQN VSEEALRIIR EAAENIRDYH ERQKRESWII AKEDGTMLGQ KITPLDAVGL
     YVPGGTAAYP SSVLMNVIPA QVAGVKRIVI TSPPNKNGTL PAGVLVAASE LGVKEIYKVG
     GAQAIAALAY GTETIRPVDK IFGPGNIYVA LAKREVFGQV AIDMIAGPSE IVVLADETAN
     VNEIAADLLS QAEHDERASA ILVTPSMKLA LAVASEVKKQ LETLPRKAIA VSALENYGAI
     YVTETLAEAV EVVNELAPEH LEVMTAEPMQ LLGQIRHAGA IFLGRFSSEP VGDYFAGPNH
     VLPTNGTARF SSGLSVDEFV KKSSIIFYSE PALQRNAGKI AAFARLEGLE AHARAVEERF
     KK
//

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