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Database: UniProt
Entry: R0KQX6_NOSB1
LinkDB: R0KQX6_NOSB1
Original site: R0KQX6_NOSB1 
ID   R0KQX6_NOSB1            Unreviewed;       385 AA.
AC   R0KQX6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histidinol dehydrogenase {ECO:0000256|ARBA:ARBA00012965};
DE            EC=1.1.1.23 {ECO:0000256|ARBA:ARBA00012965};
DE   Flags: Fragment;
GN   Name=HISX {ECO:0000313|EMBL:EOB13141.1};
GN   ORFNames=NBO_160g0002 {ECO:0000313|EMBL:EOB13141.1};
OS   Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite)
OS   (Pebrine of silkworm).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578461 {ECO:0000313|EMBL:EOB13141.1, ECO:0000313|Proteomes:UP000016927};
RN   [1] {ECO:0000313|EMBL:EOB13141.1, ECO:0000313|Proteomes:UP000016927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQ1 / CVCC 102059 {ECO:0000313|Proteomes:UP000016927};
RX   PubMed=23496955; DOI=10.1186/1471-2164-14-186;
RA   Pan G., Xu J., Li T., Xia Q., Liu S.L., Zhang G., Li S., Li C., Liu H.,
RA   Yang L., Liu T., Zhang X., Wu Z., Fan W., Dang X., Xiang H., Tao M., Li Y.,
RA   Hu J., Li Z., Lin L., Luo J., Geng L., Wang L., Long M., Wan Y., He N.,
RA   Zhang Z., Lu C., Keeling P.J., Wang J., Xiang Z., Zhou Z.;
RT   "Comparative genomics of parasitic silkworm microsporidia reveal an
RT   association between genome expansion and host adaptation.";
RL   BMC Genomics 14:186-186(2013).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001654};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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|ARBA:ARBA00004940}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|RuleBase:RU004175}.
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DR   EMBL; KB909068; EOB13141.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0KQX6; -.
DR   STRING; 578461.R0KQX6; -.
DR   EnsemblFungi; EOB13141; EOB13141; NBO_160g0002.
DR   VEuPathDB; MicrosporidiaDB:NBO_160g0002; -.
DR   HOGENOM; CLU_006732_3_0_1; -.
DR   OMA; YIAGPNH; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000016927; Unassembled WGS sequence.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|PIRSR:PIRSR000099-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016927};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   ACT_SITE        295
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        296
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOB13141.1"
FT   NON_TER         385
FT                   /evidence="ECO:0000313|EMBL:EOB13141.1"
SQ   SEQUENCE   385 AA;  40499 MW;  5C1ABBCE374C905C CRC64;
     ISKTVSEILN NVKDNGDAAL REYGAKFDKT DVKALKVSDE EIAAAGARLS DELKQAMAVA
     VKNIETFHNA QRLQAVDVET LPGVRCQQVT RPIASVGLYI PGGSAPLFST VLMLATPARI
     AGCQQVVLCS PAPIADEILY AAQLCGVRNI FNVAGAQAIA DLAFGTESVA KVDKIFGPGN
     AFVTEAKRQV SQRLDGAAID MPAGPSEVLV IADSGATPDF VASDLLSQAE HGPDSQVILL
     TPDSEMATRV AQAVERQLAA LSRAETARGA LSASRIIVAR DIAQCVEISN QYGPEHLIIQ
     TRNARELVDG ITSAGSVFLG DWSPESAGDY ASGTNHVLPT YGYTATCSSL GLADFQKRMT
     VQELSRDGFA ALASTIEILA AAERL
//
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