ID   A5EAG1_BRASB            Unreviewed;       431 AA.
AC   A5EAG1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024};
DE            Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024};
DE            EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024,
GN   ECO:0000313|EMBL:ABQ33155.1};
GN   OrderedLocusNames=BBta_0897 {ECO:0000313|EMBL:ABQ33155.1};
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ33155.1, ECO:0000313|Proteomes:UP000000246};
RN   [1] {ECO:0000313|EMBL:ABQ33155.1, ECO:0000313|Proteomes:UP000000246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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}.
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};
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-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}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|HAMAP-Rule:MF_01024,
CC       ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}.
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DR   EMBL; CP000494; ABQ33155.1; -; Genomic_DNA.
DR   RefSeq; WP_012041205.1; NC_009485.1.
DR   AlphaFoldDB; A5EAG1; -.
DR   STRING; 288000.BBta_0897; -.
DR   KEGG; bbt:BBta_0897; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_3_5; -.
DR   OrthoDB; 9805269at2; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000000246; 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   Gene3D; 1.20.5.1300; -; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
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   NCBIfam; TIGR00069; hisD; 1.
DR   PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PIRSF; PIRSF000099; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01024};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01024};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}.
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   BINDING         130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         214
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         420
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
SQ   SEQUENCE   431 AA;  45076 MW;  2C77F0E4C8FF11EC CRC64;
     MPIRLSRAHA DFDAQFRQFL AAKRETSADV EAAARAIVDD VAKRGDAALL EATRKFDRLE
     LTAASLRVTA DEIEAAVTAC DAATLDALKF ARDRIEAFHL KQLPQDQRFT DAAGVELGWR
     WSAIESAGLY VPGGTAAYPS SVLMNAIPAK VAGVSRLVMV VPAPDGKLNP LVLAAAHLGG
     VSEIYRVGGA QAVAALAHGT ATIAPVVKIV GPGNAYVAAA KRLVFGKVGI DMIAGPSEVL
     VIADDSGNAD WIAADLLAQA EHDASAQSIL ITDSRRLADD VARAVEGQLK TLPRAQIAGA
     SWADFGAIIE VEDLDQAVPL ADAIAAEHLE IMTRDPDAFA ARVRNAGAIF LGAHTPEAIG
     DYVGGSNHVL PTARSARFSS GLGVLDFMKR TSLLKCGPEQ LRALGPAAMT LGKAEGLDAH
     SRSVGIRLNL P
//