Q9RQ88 (HISX_BUCDN) 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

Organism

Buchnera aphidicola subsp. Diuraphis noxia

Taxonomic identifier

118101 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	201 AA.
Sequence status	Fragment.
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
Subunit structure	Homodimer By similarity. 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
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 – ›201	›201	Histidinol dehydrogenase HAMAP MF_01024		PRO_0000135744
Experimental info
	Non-terminal residue	201	1

Sequences

	Sequence		Length	Mass (Da)
	Q9RQ88 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 24DD9DAED0371334	FASTA	201	22,605
	10 20 30 40 50 60 MNYLKNIFYW SKLNYDEQQK ILSRPILNRN HTVKDTVKKV IENVKNFGDN ALRKYSILFD 70 80 90 100 110 120 KFNVNEFRIP EEKIISSFLN INENLKSSIL IAKKNITSFH EAQILSTIDI ETQIGVRCQQ 130 140 150 160 170 180 VYLPLNSVGI YIPNGTTSLF SSVLMLAIPA KIAGCKEIIL CSPPPINNNI LYASYVCGIK 190 200 KIFQVGGAQA IAALAFGTET 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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF129281 Genomic DNA. Translation: AAF13770.1.
3D structure databases
ProteinModelPortal	Q9RQ88.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_01024. HisD. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR012131. Hstdl_DH. [Graphical view]
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PRINTS	PR00083. HOLDHDRGNASE.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HISX_BUCDN

Accession

Primary (citable) accession number: Q9RQ88

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	May 1, 2000
Last modified:	September 21, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program