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O26327 (HISX_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length426 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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

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

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135899

Sites

Active site3231Proton acceptor By similarity
Active site3241Proton acceptor By similarity
Metal binding2551Zinc By similarity
Metal binding2581Zinc By similarity
Metal binding3571Zinc By similarity
Metal binding4161Zinc By similarity
Binding site1251NAD By similarity
Binding site1871NAD By similarity
Binding site2101NAD By similarity
Binding site2331Substrate By similarity
Binding site2551Substrate By similarity
Binding site2581Substrate By similarity
Binding site3241Substrate By similarity
Binding site3571Substrate By similarity
Binding site4111Substrate By similarity
Binding site4161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O26327 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A9A0F2AA25B8594A

FASTA42646,420
        10         20         30         40         50         60 
MLMKITEFDY RRISELVERA RLDVDDVLGP VADIISMVRD GGDDALRELT GRFDGVTVEN 

        70         80         90        100        110        120 
FRVSREEIEE AHKNLEPGVK EALREAASNI EEFHRMQMPS GWMSEVRPGV MAGQLVRPID 

       130        140        150        160        170        180 
SVGCYIPGGR AVYPSTILMT VIPARIAGVE RIVCCTPPAQ DGSVPDAVLV AADMAGASEI 

       190        200        210        220        230        240 
YRVGGAQAVA AMAYGTETIR PVDKIVGPGN IFVTAAKKLV YGEVDIDFPA GPSEVLIIAD 

       250        260        270        280        290        300 
ETASPEYIAL EILAQAEHDP QAASVLVTDS RDLALEVKEM VHENIKYMER ANIIRESLER 

       310        320        330        340        350        360 
YGMIVLTADI DEAVDFSNAY APEHLVIMTD SPEETLEGIR NAGSIFLGEL SPVAAGDYGS 

       370        380        390        400        410        420 
GTNHVLPTSG CARMYSGLST ESFIKKPTVQ RITKEGLRNL QGTVLKLAEY EGLHAHAESF 


RRRLRD 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB84731.1.
PIRH69127.
RefSeqNP_275368.1. NC_000916.1.

3D structure databases

ProteinModelPortalO26327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH225.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB84731; AAB84731; MTH_225.
GeneID1470186.
KEGGmth:MTH225.

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAPSEILII.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-225-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 nameHISX_METTH
AccessionPrimary (citable) accession number: O26327
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways