Reviewed, UniProtKB/Swiss-Prot P60858 (HISX_CORDI)

Names and origin

Protein names

Recommended name:
    Histidinol dehydrogenase
      Short name=HDH
    EC=1.1.1.23

Gene names

Name:	hisD
Ordered Locus Names:	DIP1566

Organism

Corynebacterium diphtheriae [Complete proteome] [HAMAP]

Taxonomic identifier

1717 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity.
Catalytic activity	L-histidinol + 2 NAD(+) = L-histidine + 2 NADH.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Sequence similarities	Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Histidinol dehydrogenase		PRO_0000135759
Sites
	Active site	343	1	Proton acceptor By similarity
	Active site	344	1	Proton acceptor By similarity
	Metal binding	274	1	Zinc By similarity
	Metal binding	277	1	Zinc By similarity
	Metal binding	377	1	Zinc By similarity
	Metal binding	436	1	Zinc By similarity
	Binding site	135	1	NAD By similarity
	Binding site	199	1	NAD By similarity
	Binding site	229	1	NAD By similarity
	Binding site	252	1	Substrate By similarity
	Binding site	274	1	Substrate By similarity
	Binding site	277	1	Substrate By similarity
	Binding site	344	1	Substrate By similarity
	Binding site	377	1	Substrate By similarity
	Binding site	431	1	Substrate By similarity
	Binding site	436	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P60858-1 [UniParc]. Last modified April 13, 2004. Version 1. Checksum: 002BB36B98F433FB	FASTA	449	47,762
	10 20 30 40 50 60 MRKRKIMLNV IDLRGHVPTT SELRRTLPRG GTDINSVLPI VEPVVTDVKN RGAAAALDYG 70 80 90 100 110 120 EKFDHVRPTS IRVPQDVIDQ ALDSLDPNVI EALKESIARV RAVHSEQLPA QHTTSFGEGA 130 140 150 160 170 180 TITEKFIPVS RVGLYAPGGN AVYPSSVIMN VVPAQEAGVE SLVVASPPQK DHGGWPHPTI 190 200 210 220 230 240 LAAAKLLGVT EVWAMGGAQA VALLAYGDDT QQNSAEVLEP VDMITGPGNI FVTAAKRLVR 250 260 270 280 290 300 GVVGIDSEAG PTEIAIVADA QANPVWIAYD LISQAEHDVL AASVLITDSE ELAQRVNEEV 310 320 330 340 350 360 AARYSVTRNA DRVSEALKGQ QSGIVLVDDL PTAVIVADAY AAEHLEIHTA ESHKVAEQIR 370 380 390 400 410 420 NAGAIFVGGY SPVPLGDYSA GSNHVLPTSG SARYSSGLST HTFLKPVNVI YYDEVALKEI 430 440 SDTVITLADA EDLPAHGEAI RTRFENLGN

References

[1]

"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129." Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. , Quail M.A., Rabbinowitsch E., Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., Parkhill J. Nucleic Acids Res. 31:6516-6523(2003) [PubMed: 14602910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX248358 Genomic DNA. Translation: CAE50091.1.
RefSeq	NP_939908.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2650755.
GenomeReviews	Gene locus DIP1566 in contig BX248353_GR.
KEGG	cdi:DIP1566.
NMPDR	fig|257309.1.peg.1499.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P60858.
Enzyme and pathway databases
BioCyc	CDIP257309:DIP1566-MON.
Family and domain databases
HAMAP	MF_01024. [Tree]
InterPro	IPR001692. Histidinol_DHase. IPR012131. Hstdl_DHase_prok. [Graphical view]
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PRINTS	PR00083. HOLDHDRGNASE.
ProDom	PD002680. Histidinol_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00069. hisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HISX_CORDI

Accession

Primary (citable) accession number: P60858

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	November 25, 2008
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)