Reviewed, UniProtKB/Swiss-Prot Q930I4 (HISX2_RHIME)

Names and origin

Protein names

Recommended name:
    Histidinol dehydrogenase 2
      Short name=HDH 2
    EC=1.1.1.23

Gene names

Name:	hisD2
Ordered Locus Names:	RA0212
ORF Names:	SMa0398

Encoded on

Plasmid pSymA (megaplasmid 1)

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	456 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.
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.
Caution	The conserved zinc-binding site Asp residue in position 381 is replaced by an Asn.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Plasmid
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 – 456	456	Histidinol dehydrogenase 2 HAMAP MF_01024		PRO_0000135833
Sites
	Active site	347	1	Proton acceptor By similarity
	Active site	348	1	Proton acceptor By similarity
	Metal binding	276	1	Zinc By similarity
	Metal binding	279	1	Zinc By similarity
	Metal binding	440	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q930I4-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 958D34D91C28DEEA	FASTA	456	48,702
	10 20 30 40 50 60 MTLRPQLARY KDKTMTSVSF YEYSKLNAEE KAALLRRSET DISGFIEKVA PILEAVRTEG 70 80 90 100 110 120 DKALARFGRE LDKADVTEAN LKVTAAEFDA AFKLVDASVL ESVQFGIDNI RKFHEEQKPE 130 140 150 160 170 180 AMWLKEIRPG AFAGDRFTPI QSVALYVPRG KGSFPSVTMM TSVPAVVAGV PNLAIVTPPA 190 200 210 220 230 240 PDGSVDAATL VAARLAGVET VYKAGGAQAV AAVAYGTETV KPALKIVGPG SPWVVAAKRS 250 260 270 280 290 300 LSGVIDTGLP AGPSEVMILA DDTVHGGLAA LDLLIEAEHG PDSSAYLVTH SGRVAEEALA 310 320 330 340 350 360 ALPEHWARMT EQRTAFSKTV LSGKTGGIVL TSSIEESYEF VNAYAPEHLE LLSEQPFIHL 370 380 390 400 410 420 GHITEASEIL MGTHTPVSIA NFSLGPNAVL PTSRWARTFG PLSVTDFVKR SSIGYVTAPA 430 440 450 YPEFARHSHN LAIYEGFSSH ALAVSPVRDA YLKKGA

References

[1]

"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. , Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R. Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006469 Genomic DNA. Translation: AAK64870.1.
PIR	D95288.
RefSeq	NP_435458.3.
3D structure databases
SMR	Q930I4. Positions 20-456.
ModBase	Search...
Genome annotation databases
GeneID	1235437.
GenomeReviews	Gene locus RA0212 in contig AE006469_GR.
KEGG	sme:SMa0398.
NMPDR	fig|266834.1.peg.212.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG329596.
OMA	KIVGPGS.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA0398-MONOMER.
BRENDA	1.1.1.23. 142.
Family and domain databases
HAMAP	MF_01024. HisD. Divergent sequence. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. 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.
TIGRFAMs	TIGR00069. hisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HISX2_RHIME

Accession

Primary (citable) accession number: Q930I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	December 1, 2001
Last modified:	February 9, 2010
This is version 60 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)