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Protein

Histidinol dehydrogenase 2

Gene

hisD2

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
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.By similarity

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi276 – 2761ZincBy similarity
Metal bindingi279 – 2791ZincBy similarity
Active sitei347 – 3471Proton acceptorBy similarity
Active sitei348 – 3481Proton acceptorBy similarity
Metal bindingi440 – 4401ZincBy similarity

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

BioCyciSMEL266834:GJF6-5220-MONOMER.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenase 2 (EC:1.1.1.23)
Short name:
HDH 2
Gene namesi
Name:hisD2
Ordered Locus Names:RA0212
ORF Names:SMa0398
Encoded oniPlasmid pSymA (megaplasmid 1)0 Publication
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001976 Componenti: Plasmid pSymA

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Histidinol dehydrogenase 2PRO_0000135833Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ930I4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiWVVAAKR.
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.

Q930I4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLRPQLARY KDKTMTSVSF YEYSKLNAEE KAALLRRSET DISGFIEKVA
60 70 80 90 100
PILEAVRTEG DKALARFGRE LDKADVTEAN LKVTAAEFDA AFKLVDASVL
110 120 130 140 150
ESVQFGIDNI RKFHEEQKPE AMWLKEIRPG AFAGDRFTPI QSVALYVPRG
160 170 180 190 200
KGSFPSVTMM TSVPAVVAGV PNLAIVTPPA PDGSVDAATL VAARLAGVET
210 220 230 240 250
VYKAGGAQAV AAVAYGTETV KPALKIVGPG SPWVVAAKRS LSGVIDTGLP
260 270 280 290 300
AGPSEVMILA DDTVHGGLAA LDLLIEAEHG PDSSAYLVTH SGRVAEEALA
310 320 330 340 350
ALPEHWARMT EQRTAFSKTV LSGKTGGIVL TSSIEESYEF VNAYAPEHLE
360 370 380 390 400
LLSEQPFIHL GHITEASEIL MGTHTPVSIA NFSLGPNAVL PTSRWARTFG
410 420 430 440 450
PLSVTDFVKR SSIGYVTAPA YPEFARHSHN LAIYEGFSSH ALAVSPVRDA

YLKKGA
Length:456
Mass (Da):48,702
Last modified:December 1, 2001 - v1
Checksum:i958D34D91C28DEEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006469 Genomic DNA. Translation: AAK64870.1.
PIRiD95288.
RefSeqiNP_435458.3. NC_003037.1.
WP_010967210.1. NC_003037.1.

Genome annotation databases

EnsemblBacteriaiAAK64870; AAK64870; SMa0398.
GeneIDi1235437.
KEGGisme:SMa0398.
PATRICi23626884. VBISinMel96828_0220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006469 Genomic DNA. Translation: AAK64870.1.
PIRiD95288.
RefSeqiNP_435458.3. NC_003037.1.
WP_010967210.1. NC_003037.1.

3D structure databases

ProteinModelPortaliQ930I4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK64870; AAK64870; SMa0398.
GeneIDi1235437.
KEGGisme:SMa0398.
PATRICi23626884. VBISinMel96828_0220.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiWVVAAKR.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciSMEL266834:GJF6-5220-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.

Entry informationi

Entry nameiHISX2_RHIME
AccessioniPrimary (citable) accession number: Q930I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The conserved zinc-binding site Asp residue in position 381 is replaced by an Asn.Curated

Keywords - Technical termi

Complete proteome, Plasmid, 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.