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Q0K687 (Q0K687_CUPNH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 56. Feed History...

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

Sequence length446 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. HAMAP-Rule MF_01024 SAAS SAAS012131

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024 SAAS SAAS012131

Cofactor

Binds 1 zinc ion per subunit By similarity. PIRSR PIRSR000099-4 HAMAP-Rule MF_01024 SAAS SAAS012131

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024 SAAS SAAS012131

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site3411Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024
Active site3421Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024
Metal binding2731Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding2761Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding3751Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding4341Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Binding site1441NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024
Binding site2051NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024
Binding site2281NAD By similarity PIRSR PIRSR000099-2 HAMAP-Rule MF_01024
Binding site2511Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2731Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2761Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3421Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3751Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site4291Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site4341Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Sequences

Sequence LengthMass (Da)Tools
Q0K687 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: EF335B2EB27D7B0F

FASTA44647,806
        10         20         30         40         50         60 
MNATEMENLP IRRLDSSKPG FAEALRQVLA FEAGEDEAID RAAAQILADV KARGDAAVLE 

        70         80         90        100        110        120 
YTRRFDRVEA SSMGALEVSQ QQLEAALEDL EPKRRAALEA AAARVRAYHE KQKIECGSHS 

       130        140        150        160        170        180 
WEYTEADGTM LGQKVTPLDR VGIYVPGGKA AYPSSVLMNA IPARVAGVKE IIMVVPTPGG 

       190        200        210        220        230        240 
VRNELVLAAA QIAGVDRVFT IGGAQAIGAL AYGTATLPQV DKIVGPGNAY VAAAKRRVFG 

       250        260        270        280        290        300 
TVGIDMIAGP SEILVICDGT TDPDWVAMDL FSQAEHDELA QSILLCPDAG YIARVEASIQ 

       310        320        330        340        350        360 
RQLGTMPRRE VIAASISGRG ALIKVRDMEE ACEIANAIAP EHLEISAENP RQWSEKIRHA 

       370        380        390        400        410        420 
GAIFLGPYTS ESLGDYCAGP NHVLPTSRTA RFSSPLGVYD FQKRSSLIEV SEGGAQMLGQ 

       430        440 
IAAELAYGEG LQAHARSAEY RFTKRS

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References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260479 Genomic DNA. Translation: CAJ94484.1.
RefSeqYP_727852.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0K687.
ModBaseSearch...

Protein-protein interaction databases

STRING381666.H16_A3416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ94484; CAJ94484; H16_A3416.
GeneID4247065.
KEGGreh:H16_A3416.
PATRIC35236377. VBIRalEut6770_3809.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPTYGYSR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-3380-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. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ0K687_CUPNH
AccessionPrimary (citable) accession number: Q0K687
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info