Reviewed, UniProtKB/Swiss-Prot Q9RQ82 (HISX_BUCMH)

Names and origin

Protein names

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

Gene names

Name:

hisD

Organism

Buchnera aphidicola subsp. Melaphis rhois

Taxonomic identifier

118103 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	201 AA.
Sequence status	Fragment.
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. HAMAP MF_01024
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. HAMAP MF_01024
Subunit structure	Homodimer By similarity.
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
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 or NADH binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›201	›201	Histidinol dehydrogenase HAMAP MF_01024		PRO_0000135745
Experimental info
	Non-terminal residue	201	1

Sequences

	Sequence		Length	Mass (Da)
	Q9RQ82-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E0FA5769CF7DB395	FASTA	201	22,028
	10 20 30 40 50 60 MKNCLKIIHW DRCSIEEREK ILSRPILDDL SAIKKQVKTI ISDVNSLGDQ ALYNYTNIFD 70 80 90 100 110 120 KIKLNNIKIS HQDLVKAELC IDVKAKNAIQ VAIDNIRTFH ISQNISTLNI EINKGIYCQQ 130 140 150 160 170 180 IVRPIGSVGL YIPGGSAPLL STVLMLAIPA RIAGCKKIVL CSPPPITNEV LYASKICGVQ 190 200 EIFQVGGAQA IAALGFGTET I

References

[1]	"Sequence evolution in bacterial endosymbionts having extreme base compositions." Clark M.A., Moran N.A., Baumann P. Mol. Biol. Evol. 16:1586-1598(1999) [PubMed: 10555290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF129283 Genomic DNA. Translation: AAF13776.1.
3D structure databases
HSSP	HSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBase	Search...
Family and domain databases
HAMAP	MF_01024. [Tree]
InterPro	IPR001692. Histidinol_DH_CS. IPR012131. Hstdl_DH_prok-type. [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]
PROSITE	PS00611. HISOL_DEHYDROGENASE. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HISX_BUCMH

Accession

Primary (citable) accession number: Q9RQ82

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 40 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)