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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: L-histidine biosynthesis

This protein is involved in step 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 1 (hisC1), Histidinol-phosphate aminotransferase 2 (hisC2)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei135NADUniRule annotation1
Binding sitei196NADUniRule annotation1
Binding sitei219NADUniRule annotation1
Binding sitei242SubstrateUniRule annotation1
Metal bindingi264ZincUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Metal bindingi267ZincUniRule annotation1
Binding sitei267SubstrateUniRule annotation1
Active sitei332Proton acceptorUniRule annotation1
Active sitei333Proton acceptorUniRule annotation1
Binding sitei333SubstrateUniRule annotation1
Metal bindingi366ZincUniRule annotation1
Binding sitei366SubstrateUniRule annotation1
Binding sitei420SubstrateUniRule annotation1
Metal bindingi425ZincUniRule annotation1
Binding sitei425SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000006821 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357941 – 436Histidinol dehydrogenaseAdd BLAST436

Proteomic databases

PRIDEiQ606Q2.

Interactioni

Protein-protein interaction databases

STRINGi243233.MCA1963.

Structurei

Secondary structure

1436
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 10Combined sources4
Helixi16 – 24Combined sources9
Helixi32 – 48Combined sources17
Helixi50 – 61Combined sources12
Helixi68 – 71Combined sources4
Helixi75 – 83Combined sources9
Helixi87 – 107Combined sources21
Beta strandi112 – 115Combined sources4
Beta strandi121 – 128Combined sources8
Beta strandi130 – 135Combined sources6
Helixi144 – 157Combined sources14
Beta strandi160 – 165Combined sources6
Helixi169 – 171Combined sources3
Helixi175 – 184Combined sources10
Beta strandi188 – 190Combined sources3
Helixi194 – 203Combined sources10
Beta strandi206 – 208Combined sources3
Beta strandi212 – 215Combined sources4
Helixi220 – 229Combined sources10
Beta strandi233 – 235Combined sources3
Beta strandi243 – 248Combined sources6
Helixi254 – 265Combined sources12
Beta strandi272 – 278Combined sources7
Helixi280 – 293Combined sources14
Helixi294 – 296Combined sources3
Helixi300 – 310Combined sources11
Beta strandi312 – 315Combined sources4
Helixi319 – 329Combined sources11
Beta strandi332 – 339Combined sources8
Helixi341 – 344Combined sources4
Helixi345 – 347Combined sources3
Beta strandi352 – 356Combined sources5
Helixi380 – 382Combined sources3
Helixi389 – 392Combined sources4
Beta strandi393 – 399Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GICX-ray2.05A/B2-422[»]
ProteinModelPortaliQ606Q2.
SMRiQ606Q2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
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.
RefSeqiWP_010961209.1. NC_002977.6.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017282 Genomic DNA. Translation: AAU92021.1.
RefSeqiWP_010961209.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GICX-ray2.05A/B2-422[»]
ProteinModelPortaliQ606Q2.
SMRiQ606Q2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243233.MCA1963.

Proteomic databases

PRIDEiQ606Q2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
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...

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: November 2, 2016
This is version 85 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

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 one 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.