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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 sitei130 – 1301NADUniRule annotation
Binding sitei191 – 1911NADUniRule annotation
Binding sitei214 – 2141NADUniRule annotation
Binding sitei237 – 2371SubstrateUniRule annotation
Metal bindingi259 – 2591ZincUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Metal bindingi262 – 2621ZincUniRule annotation
Binding sitei262 – 2621SubstrateUniRule annotation
Active sitei327 – 3271Proton acceptorUniRule annotation
Active sitei328 – 3281Proton acceptorUniRule annotation
Binding sitei328 – 3281SubstrateUniRule annotation
Metal bindingi361 – 3611ZincUniRule annotation
Binding sitei361 – 3611SubstrateUniRule annotation
Binding sitei415 – 4151SubstrateUniRule annotation
Metal bindingi420 – 4201ZincUniRule annotation
Binding sitei420 – 4201SubstrateUniRule 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

BioCyciPCAR338963:GKDU-2953-MONOMER.
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:Pcar_2688
OrganismiPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1)
Taxonomic identifieri338963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000002534 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Histidinol dehydrogenasePRO_0000135811Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi338963.Pcar_2688.

Structurei

3D structure databases

ProteinModelPortaliQ3A133.
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.

Q3A133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRLLSFDDS DFGAALGAIV ARGETPPEGV EETVAEILEA VRLQGDRALL
60 70 80 90 100
EYTTRFDGLD LTAAQLQVTA EEIEAALAAV DSESMAALQL AADRIAAFHR
110 120 130 140 150
RQKTETWLTT DEQDVMLGQM VQPLERVGIY VPGGKASYPS SVLMNAIPAK
160 170 180 190 200
VAGVAEVVMV VPMPHGEVNP HVLAAAHLAG VDRIFKIGGA QAVAALAYGT
210 220 230 240 250
ESVPRVDKIT GPGNIYVATA KKMVFGQVDI DMIAGPSEIL VINDGSGTPE
260 270 280 290 300
HIAVDLLSQA EHDELAAAIL VTTDADFGRR VQQAVEEQLA TLKRAAIARC
310 320 330 340 350
SIDAFGAILV ARDLEQAVAL SNSIAPEHLE LAVDDPFSLL PRIRHAGAIF
360 370 380 390 400
MGHHCPEAAG DYLAGPNHTL PTGGTARFFS PLGVDDFVKK SSIISFSREG
410 420 430
LDRLGRSIVH LAELEGLEAH GRSVSIRLKD S
Length:431
Mass (Da):45,770
Last modified:November 21, 2005 - v1
Checksum:i9095B283C1766595
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000142 Genomic DNA. Translation: ABA89924.1.
RefSeqiWP_011342467.1. NC_007498.2.
YP_006718465.1. NC_007498.2.

Genome annotation databases

EnsemblBacteriaiABA89924; ABA89924; Pcar_2688.
KEGGipca:Pcar_2688.
PATRICi22891754. VBIPelCar86875_2915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000142 Genomic DNA. Translation: ABA89924.1.
RefSeqiWP_011342467.1. NC_007498.2.
YP_006718465.1. NC_007498.2.

3D structure databases

ProteinModelPortaliQ3A133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338963.Pcar_2688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA89924; ABA89924; Pcar_2688.
KEGGipca:Pcar_2688.
PATRICi22891754. VBIPelCar86875_2915.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciPCAR338963:GKDU-2953-MONOMER.

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. "Complete sequence of Pelobacter carbinolicus DSM 2380."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2380 / Gra Bd 1.

Entry informationi

Entry nameiHISX_PELCD
AccessioniPrimary (citable) accession number: Q3A133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2006
Last sequence update: November 21, 2005
Last modified: March 31, 2015
This is version 72 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.