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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273))
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 sitei141 – 1411NADUniRule annotation
Binding sitei203 – 2031NADUniRule annotation
Binding sitei226 – 2261NADUniRule annotation
Binding sitei249 – 2491SubstrateUniRule annotation
Metal bindingi271 – 2711ZincUniRule annotation
Binding sitei271 – 2711SubstrateUniRule annotation
Metal bindingi274 – 2741ZincUniRule annotation
Binding sitei274 – 2741SubstrateUniRule annotation
Active sitei339 – 3391Proton acceptorUniRule annotation
Active sitei340 – 3401Proton acceptorUniRule annotation
Binding sitei340 – 3401SubstrateUniRule annotation
Metal bindingi373 – 3731ZincUniRule annotation
Binding sitei373 – 3731SubstrateUniRule annotation
Binding sitei427 – 4271SubstrateUniRule annotation
Metal bindingi432 – 4321ZincUniRule annotation
Binding sitei432 – 4321SubstrateUniRule 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

BioCyciPLUT319225:GHDM-565-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:Plut_0554
OrganismiPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273))
Taxonomic identifieri319225 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon
ProteomesiUP000002709: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Histidinol dehydrogenasePRO_0000229860Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi319225.Plut_0554.

Structurei

3D structure databases

ProteinModelPortaliQ3B5E3.
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.

Q3B5E3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPVHYRTST STIVAVLKLY RFLDDRDALF RQIGRSVDFD PEVQRAVTDI
60 70 80 90 100
LEAVRLRGDM AVLEYTERFQ GAVLTSMQVP EEDILRAREE ADPAFIRVLE
110 120 130 140 150
EAWENILRFH RHEVENSFFY EGEGGVVLGQ RVTPMDRAML YVPGGKASYP
160 170 180 190 200
SSVLMNAAPA RVAGVGEIFM TTPCDASGAV SPHILAAASV AGVTSVYRLG
210 220 230 240 250
GAQAVAAFAY GTQTIPKVDI ITGPGNKYVA LAKKQVFGHV AIDSIAGPSE
260 270 280 290 300
VVVVADDDAD AEFITMDLFA QAEHDPDASS VLITPSMRLA EEVRDLAAAR
310 320 330 340 350
VGSMLRGEVI AEALSNNGAI VVVADIEEAC RVSDMIAPEH LELHVLHPWE
360 370 380 390 400
LLASIRHAGA VFMGGYSCET VGDYYAGPNH TLPTNGTARF FSPLSVRDFV
410 420 430 440
KHTSIISYTR RQIMACGERI ASFADHEGLE AHAEAVRARL KKG
Length:443
Mass (Da):48,062
Last modified:November 22, 2005 - v1
Checksum:i7A4C8C653019BE3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000096 Genomic DNA. Translation: ABB23438.1.
RefSeqiWP_011357313.1. NC_007512.1.
YP_374481.1. NC_007512.1.

Genome annotation databases

EnsemblBacteriaiABB23438; ABB23438; Plut_0554.
GeneIDi3746220.
KEGGiplt:Plut_0554.
PATRICi21378590. VBIChlLut1287_0577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000096 Genomic DNA. Translation: ABB23438.1.
RefSeqiWP_011357313.1. NC_007512.1.
YP_374481.1. NC_007512.1.

3D structure databases

ProteinModelPortaliQ3B5E3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi319225.Plut_0554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB23438; ABB23438; Plut_0554.
GeneIDi3746220.
KEGGiplt:Plut_0554.
PATRICi21378590. VBIChlLut1287_0577.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciPLUT319225:GHDM-565-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 Pelodictyon luteolum DSM 273."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 273.

Entry informationi

Entry nameiHISX_PELLD
AccessioniPrimary (citable) accession number: Q3B5E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: January 7, 2015
This is version 68 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.