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B0KQJ5 (B0KQJ5_PSEPG) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceInferred 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. PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS022695

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS022695

Cofactor

Binds 1 zinc ion per subunit By similarity. PIRSR PIRSR000099-4 HAMAP-Rule MF_01024 SAAS SAAS022695

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. PIRNR PIRNR000099 HAMAP-Rule MF_01024 SAAS SAAS022695

Sequence similarities

Belongs to the histidinol dehydrogenase family. RuleBase RU004175 PIRNR PIRNR000099 HAMAP-Rule MF_01024

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site3331Proton acceptor By similarity HAMAP-Rule MF_01024 PIRSR PIRSR000099-1
Active site3341Proton acceptor By similarity HAMAP-Rule MF_01024 PIRSR PIRSR000099-1
Metal binding2651Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding2681Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding3671Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding4261Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Binding site1361NAD By similarity HAMAP-Rule MF_01024
Binding site1971NAD By similarity HAMAP-Rule MF_01024
Binding site2201NAD By similarity HAMAP-Rule MF_01024
Binding site2431Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2651Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2681Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3341Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3671Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site4211Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site4261Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Sequences

Sequence LengthMass (Da)Tools
B0KQJ5 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: A2FA13FFCBF97561

FASTA44147,678
        10         20         30         40         50         60 
MTVSTAIARL NAADPDFARH LDHLLSWESV SDDAVNQRVL DIIKAVRERG DAALVEFTQR 

        70         80         90        100        110        120 
FDGVDAKSIE DLILNRERLE LALTRITPIQ REALEKAANR VRMYHERQKQ DSWQYTEADG 

       130        140        150        160        170        180 
TVLGQKVTPL DRAGLYVPGG KASYPSSVLM NAIPAKVAGV AEVVMVVPTP RGEVNELVLA 

       190        200        210        220        230        240 
AACIAGVDRV FTVGGAQAVA ALAYGTESVP QVDKIVGPGN IYVATAKRHV FGQVGIDMIA 

       250        260        270        280        290        300 
GPSEILVVCD GQTDPDWIAM DLFSQAEHDE DAQAILVSPD AAFLDRVAAS IDKLMPTMER 

       310        320        330        340        350        360 
AEIIEKSING RGALIQVRDM QQAMDVANRI APEHLELSVA DPQAWLPHIR HAGAIFMGRH 

       370        380        390        400        410        420 
TSEALGDYCA GPNHVLPTSG TARFSSPLGV YDFQKRSSII FCSEQGASEL GHTASVLARG 

       430        440 
ESLTAHARSA EYRILTQDKG N 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1 EMBL ABY96883.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABY96883.1.
RefSeqYP_001667219.1. NC_010322.1.

3D structure databases

ProteinModelPortalB0KQJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76869.PputGB1_0973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY96883; ABY96883; PputGB1_0973.
GeneID5868733.
KEGGppg:PputGB1_0973.
PATRIC19928921. VBIPsePut76638_0980.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-1004-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB0KQJ5_PSEPG
AccessionPrimary (citable) accession number: B0KQJ5
Entry history
Integrated into UniProtKB/TrEMBL: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 9, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)