Q9PM77 (HISX_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	Cj1598

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
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. HAMAP MF_01024
Catalytic activity	L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP MF_01024
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP MF_01024
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 Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process 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: EC 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 HAMAP MF_01024		PRO_0000135751
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)
	Q9PM77 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 16F08561BF7DB738	FASTA	428	46,446
	10 20 30 40 50 60 MQILVYDNLD EKQKEEALKR PAISAKDEIS KIVSSIIKEV QEKGDKALIE QALKFDKAEI 70 80 90 100 110 120 SKIKITQEEI TQASNRLDKD LQEAILVAYE NIKKFHEAQI PHEIALETTK GVKCEVLTRP 130 140 150 160 170 180 IEKVGLYIPG GLAPLFSTVL MLAIPAKIAG CEKIVLASPA KINDAVLFCA KLCGVDEIYQ 190 200 210 220 230 240 MGGAGAIAAL TYGTQSVLKV 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]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL35695.1.
PIR	D81255.
RefSeq	YP_002344967.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q9PM77.
SMR	Q9PM77. Positions 3-428.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	905868.
GenomeReviews	Gene locus Cj1598 in contig AL111168_GR.
KEGG	cje:Cj1598.
PATRIC	20060156. VBICamJej33762_1574.
Phylogenomic databases
HOGENOM	HBG329596.
OMA	NRYVTEA.
ProtClustDB	PRK00877.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1598-MONOMER.
Family and domain databases
HAMAP	MF_01024. HisD. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR001692. Histidinol_DH_CS. IPR022695. Histidinol_DH_monofunct. IPR012131. Hstdl_DH. [Graphical view]
KO	K00013.
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000099. Histidinol_dh. 1 hit.
PRINTS	PR00083. HOLDHDRGNASE.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00069. HisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HISX_CAMJE

Accession

Primary (citable) accession number: Q9PM77
Secondary accession number(s): Q0P830

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program