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
//