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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Brucella suis biovar 1 (strain 1330)
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

Pathway:iL-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 regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  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 (hisC)
  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)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

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:BR0252, BS1330_I0253
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000007104 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Histidinol dehydrogenasePRO_0000135741Add
BLAST

Interactioni

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi12 – 209Combined sources
Helixi30 – 4415Combined sources
Helixi46 – 5712Combined sources
Helixi61 – 644Combined sources
Helixi70 – 7910Combined sources
Helixi82 – 10019Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi125 – 1306Combined sources
Helixi134 – 1363Combined sources
Helixi139 – 15214Combined sources
Beta strandi155 – 1606Combined sources
Helixi164 – 1663Combined sources
Helixi170 – 1789Combined sources
Beta strandi183 – 1864Combined sources
Helixi189 – 19810Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi207 – 2104Combined sources
Helixi215 – 22410Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi245 – 2473Combined sources
Helixi249 – 26012Combined sources
Beta strandi267 – 2737Combined sources
Helixi275 – 29117Combined sources
Helixi296 – 30510Combined sources
Beta strandi307 – 3104Combined sources
Helixi314 – 32411Combined sources
Beta strandi327 – 3337Combined sources
Helixi336 – 3383Combined sources
Turni339 – 3424Combined sources
Beta strandi347 – 3526Combined sources
Helixi357 – 3626Combined sources
Beta strandi364 – 3663Combined sources
Helixi375 – 3773Combined sources
Helixi384 – 3874Combined sources
Beta strandi388 – 3958Combined sources
Helixi398 – 41417Combined sources
Helixi418 – 43013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G07X-ray1.95A1-430[»]
4G09X-ray1.90A1-430[»]
ProteinModelPortaliQ8G2R2.
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.

Q8G2R2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL
60 70 80 90 100
DYSRRFDRID LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA
110 120 130 140 150
RQLPKDDRYT DALGVELGSR WTAIEAVGLY VPGGTASYPS SVLMNAMPAK
160 170 180 190 200
VAGVDRIVMV VPAPDGNLNP LVLVAARLAG VSEIYRVGGA QAIAALAYGT
210 220 230 240 250
ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL IVADKDNNPD
260 270 280 290 300
WIAADLLAQA EHDTAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA
310 320 330 340 350
SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF
360 370 380 390 400
IGGYTPEVIG DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ
410 420 430
LRALGPAAIE IARAEGLDAH AQSVAIRLNL
Length:430
Mass (Da):46,072
Last modified:March 1, 2003 - v1
Checksum:i2752FA59731001E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29201.1.
CP002997 Genomic DNA. Translation: AEM17614.1.
RefSeqiWP_004687945.1. NZ_KN046804.1.

Genome annotation databases

EnsemblBacteriaiAAN29201; AAN29201; BR0252.
AEM17614; AEM17614; BS1330_I0253.
KEGGibms:BR0252.
bsi:BS1330_I0253.
PATRICi17788781. VBIBruSui107850_0261.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29201.1.
CP002997 Genomic DNA. Translation: AEM17614.1.
RefSeqiWP_004687945.1. NZ_KN046804.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G07X-ray1.95A1-430[»]
4G09X-ray1.90A1-430[»]
ProteinModelPortaliQ8G2R2.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ8G2R2.
ChEMBLiCHEMBL5431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN29201; AAN29201; BR0252.
AEM17614; AEM17614; BS1330_I0253.
KEGGibms:BR0252.
bsi:BS1330_I0253.
PATRICi17788781. VBIBruSui107850_0261.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Miscellaneous databases

PROiQ8G2R2.

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: 1330.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.

Entry informationi

Entry nameiHISX_BRUSU
AccessioniPrimary (citable) accession number: Q8G2R2
Secondary accession number(s): G0KBV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: July 22, 2015
This is version 93 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

Documents

  1. Brucella suis
    Brucella suis (strain 1330): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.