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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351NADUniRule annotation
Binding sitei196 – 1961NADUniRule annotation
Binding sitei219 – 2191NADUniRule annotation
Binding sitei242 – 2421SubstrateUniRule annotation
Metal bindingi264 – 2641ZincUniRule annotation
Binding sitei264 – 2641SubstrateUniRule annotation
Metal bindingi267 – 2671ZincUniRule annotation
Binding sitei267 – 2671SubstrateUniRule annotation
Active sitei332 – 3321Proton acceptorUniRule annotation
Active sitei333 – 3331Proton acceptorUniRule annotation
Binding sitei333 – 3331SubstrateUniRule annotation
Metal bindingi366 – 3661ZincUniRule annotation
Binding sitei366 – 3661SubstrateUniRule annotation
Binding sitei420 – 4201SubstrateUniRule annotation
Metal bindingi425 – 4251ZincUniRule annotation
Binding sitei425 – 4251SubstrateUniRule annotation

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:MCA1963
OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Taxonomic identifieri243233 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
ProteomesiUP000006821: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Histidinol dehydrogenasePRO_0000135794Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243233.MCA1963.

Structurei

Secondary structure

1
436
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Helixi16 – 249Combined sources
Helixi32 – 4817Combined sources
Helixi50 – 6112Combined sources
Helixi68 – 714Combined sources
Helixi75 – 839Combined sources
Helixi87 – 10721Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi121 – 1288Combined sources
Beta strandi130 – 1356Combined sources
Helixi144 – 15714Combined sources
Beta strandi160 – 1656Combined sources
Helixi169 – 1713Combined sources
Helixi175 – 18410Combined sources
Beta strandi188 – 1903Combined sources
Helixi194 – 20310Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi212 – 2154Combined sources
Helixi220 – 22910Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi243 – 2486Combined sources
Helixi254 – 26512Combined sources
Beta strandi272 – 2787Combined sources
Helixi280 – 29314Combined sources
Helixi294 – 2963Combined sources
Helixi300 – 31011Combined sources
Beta strandi312 – 3154Combined sources
Helixi319 – 32911Combined sources
Beta strandi332 – 3398Combined sources
Helixi341 – 3444Combined sources
Helixi345 – 3473Combined sources
Beta strandi352 – 3565Combined sources
Helixi380 – 3823Combined sources
Helixi389 – 3924Combined sources
Beta strandi393 – 3997Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GICX-ray2.05A/B2-422[»]
ProteinModelPortaliQ606Q2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q606Q2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEVKIKRLY TGDADFASQL DRLLAWSESE DTDIHQRVTE IIGCIRRDGD
60 70 80 90 100
AALVELTARF DHFVVDTAAA LELPRDVLEA AWQALPAEQA KALREAAERI
110 120 130 140 150
RAYAERQKLD SWDYREADGT LLGQKITPLD RVGLYVPGGK AAYPSSVLMN
160 170 180 190 200
AVPAKVAGVP ELIMAVPAPR GELNALVLAA AYISGVDRVF RIGGAQAVAA
210 220 230 240 250
LAYGTETVPR VDKIVGPGNI YVATAKKLVF GQVGIDMVAG PSEILVISDG
260 270 280 290 300
RTDPDWIAMD LFSQAEHDED AQAILISPDA AHLEAVQASI ERLLPGMERA
310 320 330 340 350
EVIRTSLERR GGMILVDDLE QAAAVANRIA PEHLELSVES PEVLVESIRN
360 370 380 390 400
AGAIFMGRYT AEALGDYCAG PNHVLPTSGT ARFSSPLGVY DFQKRSSLIY
410 420 430
CSPDGADQLG RTASLLAWGE GLGAHARSAE YRIRHH
Length:436
Mass (Da):47,045
Last modified:November 23, 2004 - v1
Checksum:i161D3DEAAE8BDE17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017282 Genomic DNA. Translation: AAU92021.1.
RefSeqiYP_114396.1. NC_002977.6.

Genome annotation databases

EnsemblBacteriaiAAU92021; AAU92021; MCA1963.
GeneIDi3102435.
KEGGimca:MCA1963.
PATRICi22607774. VBIMetCap22254_1995.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017282 Genomic DNA. Translation: AAU92021.1.
RefSeqiYP_114396.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GICX-ray2.05A/B2-422[»]
ProteinModelPortaliQ606Q2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243233.MCA1963.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU92021; AAU92021; MCA1963.
GeneIDi3102435.
KEGGimca:MCA1963.
PATRICi22607774. VBIMetCap22254_1995.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33009 / NCIMB 11132 / Bath.

Entry informationi

Entry nameiHISX_METCA
AccessioniPrimary (citable) accession number: Q606Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: January 7, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.