Reviewed, UniProtKB/Swiss-Prot Q5HSJ3 (HISX_CAMJR)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	CJE1770

Organism

Campylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]

Taxonomic identifier

195099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	428 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 – 428	428	Histidinol dehydrogenase		PRO_0000135752
Sites
	Active site	323	1	Proton acceptor By similarity
	Active site	324	1	Proton acceptor By similarity
	Metal binding	256	1	Zinc By similarity
	Metal binding	259	1	Zinc By similarity
	Metal binding	357	1	Zinc By similarity
	Metal binding	416	1	Zinc By similarity
	Binding site	234	1	Substrate By similarity
	Binding site	256	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity
	Binding site	324	1	Substrate By similarity
	Binding site	357	1	Substrate By similarity
	Binding site	411	1	Substrate By similarity
	Binding site	416	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HSJ3-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: EF20C2265EBABBE6	FASTA	428	46,430
	10 20 30 40 50 60 MQILVYDNLD EKQKEEALKR PAISAKDEIS KIVSSIIKEV QEKGDEALIE QALKFDKAEI 70 80 90 100 110 120 SKIKITQEEI TQASKRLDKD LQEAILVAYE NIKKFHEAQI PHEIALETTK GVKCEVLTRP 130 140 150 160 170 180 IEKVGLYIPG GLAPLFSTVL MLAIPAKIAG CEKIVLASPA KINDAVLFCA KLCGVDEIYQ 190 200 210 220 230 240 MGGAGAIAAL AYGTQSVLKV DKIFGPGNAF VTEAKRQVSS DINGAAIDMQ AGPSEVLVIA 250 260 270 280 290 300 DDLANEKFVA SDLLSQAEHG ADSQVILVCL SQDFAKKASD EVQSQLELLP RKELASKSIA 310 320 330 340 350 360 NSRIIIAKDL NQALEISNLY APEHLIIQTQ NPRELLKGVK HAGSVFLGAY SPESMGDYAS 370 380 390 400 410 420 GTNHVLPTYG LTKTHSSLGL ADFSKRMTVQ ELSKEGFLAL GKSVEILAQN EHLDAHKNAV TFRLESLK

References

[1]

"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species." Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. , Badger J.H., Fraser C.M., Nelson K.E. PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000025 Genomic DNA. Translation: AAW36194.1.
RefSeq	YP_179742.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3232397.
GenomeReviews	Gene locus CJE1770 in contig CP000025_GR.
KEGG	cjr:CJE1770.
NMPDR	fig|195099.3.peg.1298.
TIGR	CJE1770.
Phylogenomic databases
HOGENOM	Q5HSJ3.
Enzyme and pathway databases
BioCyc	CJEJ195099:CJE_1770-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_CAMJR

Accession

Primary (citable) accession number: Q5HSJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	February 15, 2005
Last modified:	November 25, 2008
This is version 28 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)