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Reviewed, UniProtKB/Swiss-Prot Q988P7 (HISX2_RHILO)

Last modified June 16, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Histidinol dehydrogenase 2
      Short name=HDH 2
    EC=1.1.1.23
Gene names
Name: hisD2
Ordered Locus Names: mlr6649
OrganismRhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier381 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium

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Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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

Sequence similarities

Belongs to the histidinol dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Histidinol dehydrogenase 2 HAMAP MF_01024
PRO_0000135830

Sites

Active site3811Proton acceptor By similarity
Active site3821Proton acceptor By similarity
Metal binding3131Zinc By similarity
Metal binding3161Zinc By similarity
Metal binding4151Zinc By similarity
Metal binding4751Zinc By similarity
Binding site1841NAD By similarity
Binding site2451NAD By similarity
Binding site2681NAD By similarity
Binding site2911Substrate By similarity
Binding site3131Substrate By similarity
Binding site3161Substrate By similarity
Binding site3821Substrate By similarity
Binding site4151Substrate By similarity
Binding site4701Substrate By similarity
Binding site4751Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q988P7-1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 71446C53BBF5D9F4

FASTA50054,015
        10         20         30         40         50         60 
MPPAGGIFHR PPTTRKSRRL TPRSACSNST CSRTWGEQPW LLALHSIDSD RNAGRRPCKR 

        70         80         90        100        110        120 
RAIAMIRTIK SARGSVVNGG NGAMTSAVQT LLDQVEQGGD RAVRELSIRF DKFDRDSYRL 

       130        140        150        160        170        180 
TKAEIDACIN SLTGREREDL DFAQDQIRNF AEAQRATLLD LEIETLPGVV LGHRNVPIQN 

       190        200        210        220        230        240 
VGCYVPGGKY PLLASAHMTV LTARVAGCER IITCAPPFQG KVAEKIVAAQ ALAGADEIYC 

       250        260        270        280        290        300 
LGGVQAIAAM AYGTETIAPV DMVAGPGNAY VAEAKRLLFG KVGIDLFAGP TETLVIADDS 

       310        320        330        340        350        360 
VDGELVATDL LGQAEHGVNS PAVLITNSEK LALDTVAEIG RLLTILPTAA IAAKAWEDFG 

       370        380        390        400        410        420 
EIILCETTKE MVAEADRLAS EHVQVMTRDP DHFLNSMRNY GALFLGARTN VSFGDKVIGT 

       430        440        450        460        470        480 
NHTLPTNKAA RYTGGLWVGK FLKTCTYQRI LTDEASALIG EYGSRLSLME GFVGHAEQSN 

       490        500 
IRVRRYGGRN VGYAMPVDPR

« Hide

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References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

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Cross-references

Sequence databases

BA000012 Genomic DNA. Translation: BAB52900.1.
RefSeqNP_107114.1.

3D structure databases

HSSPHSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBaseSearch...

Genome annotation databases

GeneID1229769.
GenomeReviewsGene locus mlr6649 in contig BA000012_GR.
KEGGmlo:mlr6649.
NMPDRfig|266835.1.peg.5215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ988P7.
OMAQ988P7. NVGCYVP.

Enzyme and pathway databases

BRENDA1.1.1.23. 3315.

Family and domain databases

HAMAPMF_01024. Divergent sequence.
[Tree]
InterProIPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH_prok-type.
[Graphical view]
PANTHERPTHR21256:SF2. Hstdl_DH_prok. 1 hit.
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSPR00083. HOLDHDRGNASE.
ProDomPD002680. Histidinol_dh. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHISX2_RHILO
AccessionPrimary (citable) accession number: Q988P7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2001
Last modified: June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents