GenomeNet

Database: UniProt
Entry: A0A0F7HN99_9STAP
LinkDB: A0A0F7HN99_9STAP
Original site: A0A0F7HN99_9STAP 
ID   A0A0F7HN99_9STAP        Unreviewed;       410 AA.
AC   A0A0F7HN99;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Histidinol dehydrogenase {ECO:0000313|EMBL:AKG75112.1};
GN   ORFNames=AAT16_13485 {ECO:0000313|EMBL:AKG75112.1};
OS   Salinicoccus halodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX   NCBI_TaxID=407035 {ECO:0000313|EMBL:AKG75112.1, ECO:0000313|Proteomes:UP000034029};
RN   [1] {ECO:0000313|EMBL:AKG75112.1, ECO:0000313|Proteomes:UP000034029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3B36 {ECO:0000313|EMBL:AKG75112.1,
RC   ECO:0000313|Proteomes:UP000034029};
RX   PubMed=26634017;
RA   Jiang K., Xue Y., Ma Y.;
RT   "Complete genome sequence of Salinicoccus halodurans H3B36, isolated from
RT   the Qaidam Basin in China.";
RL   Stand. Genomic Sci. 10:116-116(2015).
RN   [2] {ECO:0000313|Proteomes:UP000034029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3B36 {ECO:0000313|Proteomes:UP000034029};
RA   Ma Y., Jiang K., Xue Y.;
RT   "Complete genome sequence of Salinicoccus halodurans strain H3B36, isolated
RT   from the Qaidam basin of China.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000099-4};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000099-4};
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|RuleBase:RU004175}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011366; AKG75112.1; -; Genomic_DNA.
DR   RefSeq; WP_046791289.1; NZ_FOTB01000002.1.
DR   AlphaFoldDB; A0A0F7HN99; -.
DR   STRING; 407035.AAT16_13485; -.
DR   KEGG; shv:AAT16_13485; -.
DR   PATRIC; fig|407035.3.peg.2777; -.
DR   OrthoDB; 9805269at2; -.
DR   Proteomes; UP000034029; Chromosome.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
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:InterPro.
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   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   ECO:0000256|PIRSR:PIRSR000099-4};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000099};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000099-4}.
FT   ACT_SITE        308
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         401
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         401
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
SQ   SEQUENCE   410 AA;  45727 MW;  0DD92471DDD9DFFE CRC64;
     MKASEFREVF QNNTETAGFE GMGDVMAIIE EVRQNKDAAL RQYTEKFDGR SPASFQVPAE
     HLEESYNALP EAEKQALEKI RERIESYQKT IRYQNRDDGE FKYVYHPLEK VGVYVPGGTA
     LYPSSVLMTV VPALVAGVDE IHVVTPTFEE NNITFAALHI CGVKNVYTVG GAHAIAALAY
     GTESIPKVDK IVGPGNYYVA LAKRLLFGEV GIDMIAGPSE ILIYIDSDVN VDAIVYDIFA
     QSEHDANART FLLSENQEII DTIKSRINML IDSQPRVEII KKSLENNHYA VVDSREQLLE
     LINHIAPEHV SIQHKDSEMI IRNIKYAGAV FEGYYSPEAI GDYAAGPSHV LPTDRTGRFS
     HGLNVNDFLT SHAVISLEES TFDDIAEPAM AVARREQLDA HYQSLKIRTE
//
DBGET integrated database retrieval system