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HISX_STAAB
ID   HISX_STAAB              Reviewed;         416 AA.
AC   Q2YZB4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024};
DE            Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024};
DE            EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024};
GN   Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; OrderedLocusNames=SAB2554c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC       {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_01024};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01024};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01024}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01024}.
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DR   EMBL; AJ938182; CAI82242.1; -; Genomic_DNA.
DR   RefSeq; WP_000930658.1; NC_007622.1.
DR   AlphaFoldDB; Q2YZB4; -.
DR   SMR; Q2YZB4; -.
DR   KEGG; sab:SAB2554c; -.
DR   HOGENOM; CLU_006732_3_3_9; -.
DR   OMA; MVTGPGN; -.
DR   UniPathway; UPA00031; UER00014.
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;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW   Oxidoreductase; Zinc.
FT   CHAIN           1..416
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000229866"
FT   ACT_SITE        314
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   ACT_SITE        315
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ   SEQUENCE   416 AA;  46206 MW;  D05A097D8E2860C5 CRC64;
     MLNAQQFLNQ FSLEAPLDES LYPIIRDICQ EVKVHGDKAL KMYNLTFDHT KTDHLEISHE
     QIKAAFDTLD EKTKQALQQS YERIKAYQES IKQTNQQLEK SVECYEIYHP LESVGIYVPG
     GKASYPSTVL MTATLAQVAG VENIVVVTPP QPNGVSQEVL AACYITQVNQ VFQVGGAQSI
     AALTYGTETI PKVDKIVGPG NQFVAYAKKY LFGQVGIDQI AGPTEIALII DDTADLDAIV
     YDVFAQAEHD ELARTYVISE DAQVLKDLES RITKALPNVD RYDIVSKSIA NQHYLIHASN
     FDDACHVMNT IAPEHASIQT VNPQPYIEKV KYVGALFIGH YSPEVIGDYV AGPSHVLPTN
     RTARFTNGLS VNDFLTRNTV IHLSKDTFEQ IADSAQHIAH VEALYNHQQS ILIRQS
 
 
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