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UniProtKB/Swiss-Prot entry Q8NNT5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HISX_CORGL
Primary accession number Q8NNT5
Secondary accession number Q9KJU2
Integrated into Swiss-Prot on March 25, 2003
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 47)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: Cgl2102, cg2305
From
Corynebacterium glutamicum (Brevibacterium flavum) [TaxID: 1718] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
Chun J.Y., Han M.S., Sim J.K., Lee M.-S.;
"Molecular cloning of hisD gene from Corynebacterium glutamicum.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
Nakagawa S.;
"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan]
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins.";
J. Biotechnol. 104:5-25(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF160480; AAF80392.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAB99495.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927154; CAF20438.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_601301.1; -.
YP_226339.1; -.
3D structure databases
HSSP P06988; 1K75. [HSSP ENTRY / PDB]
ModBase Q8NNT5.
Enzyme and pathway databases
BioCyc CGLU196627-1:CG2305-MON; -.
Ontologies
GO
GO:0004399; Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01024; -; 1.
PBIL [Tree]
InterPro IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
Graphical view of domain structure.
PANTHER PTHR21256:SF2; Hstdl_DH_prok; 1.
Pfam PF00815; Histidinol_dh; 1.
Pfam graphical view of domain structure.
PRINTS PR00083; HOLDHDRGNASE.
ProDom PD002680; Histidinol_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00069; hisD; 1.
PROSITE PS00611; HISOL_DEHYDROGENASE; 1.
Genome annotation databases
GeneID 1020053; -.
3343227; -.
GenomeReviews BA000036_GR; Cgl2102.
BX927147_GR; cg2305.
KEGG cgb:cg2305; -.
cgl:NCgl2021; -.
Phylogenomic databases
HOGENOM Q8NNT5; -.
Genome annotation databases
CMR Q8NNT5; Cgl2102.
Other
ProtoNet Q8NNT5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   442  442     Histidinol dehydrogenase. PRO_0000135761
ACT_SITE   332   332        Proton acceptor (By similarity). 
ACT_SITE   333   333        Proton acceptor (By similarity). 
METAL   263   263        Zinc (By similarity). 
METAL   266   266        Zinc (By similarity). 
METAL   366   366        Zinc (By similarity). 
METAL   425   425        Zinc (By similarity). 
BINDING   129   129        NAD (By similarity). 
BINDING   193   193        NAD (By similarity). 
BINDING   218   218        NAD (By similarity). 
BINDING   241   241        Substrate (By similarity). 
BINDING   263   263        Substrate (By similarity). 
BINDING   266   266        Substrate (By similarity). 
BINDING   333   333        Substrate (By similarity). 
BINDING   366   366        Substrate (By similarity). 
BINDING   420   420        Substrate (By similarity). 
BINDING   425   425        Substrate (By similarity). 
CONFLICT   372   380        Missing (in Ref. 1). 
Sequence information
Length: 442 AA [This is the length of the unprocessed precursor] Molecular weight: 46771 Da [This is the MW of the unprocessed precursor] CRC64: D696294519F95838 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLNVTDLRGQ TPSKSDIRRA LPRGGTDVWS VLPIVQPVVE DVQNRGAEAA LDYGEKFDHI 

        70         80         90        100        110        120 
RPASVRVPAE VIAAAENTLD PLVRESIEES IRRVRKVHAE QKPSEHTTEL SPGGTVTERF 

       130        140        150        160        170        180 
MPIDRVGLYV PGGNAVYPSS VIMNTVPAQE AGVNSLVVAS PPQAEHGGWP HPTILAACSI 

       190        200        210        220        230        240 
LGVDEVWAVG GGQAVALLAY GDDAAGLEPV DMITGPGNIF VTAAKRLVRG VVGTDSEAGP 

       250        260        270        280        290        300 
TEIAVLADAS ANAVNVAYDL ISQAEHDVMA ASVLITDSEQ LAKDVNREIE ARYSITRNAE 

       310        320        330        340        350        360 
RVAEALRGAQ SGIVLVDDIS VGIQVADQYA AEHLEIHTEN ARAVAEQITN AGAIFVGDFS 

       370        380        390        400        410        420 
PVPLGDYSAG SNHVLPTSGS ARFSAGLSTH TFLRPVNLIE YDEAALKDVS QVVINFANAE 

       430        440 
DLPAHGEAIR ARFENLPTTD EA
Q8NNT5 in FASTA format

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