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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

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 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)DescriptionActionsGraphical viewLength
Binding sitei130NADUniRule annotation1
Binding sitei191NADUniRule annotation1
Binding sitei214NADUniRule annotation1
Binding sitei237SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Active sitei327Proton acceptorUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Metal bindingi361ZincUniRule annotation1
Binding sitei361SubstrateUniRule annotation1
Binding sitei415SubstrateUniRule annotation1
Metal bindingi420ZincUniRule annotation1
Binding sitei420SubstrateUniRule 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:BR0252, BS1330_I0253
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000007104 Componenti: Chromosome I

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5431.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357411 – 430Histidinol dehydrogenaseAdd BLAST430

Interactioni

Chemistry databases

BindingDBiQ8G2R2.

Structurei

Secondary structure

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 20Combined sources9
Helixi30 – 44Combined sources15
Helixi46 – 57Combined sources12
Helixi61 – 64Combined sources4
Helixi70 – 79Combined sources10
Helixi82 – 100Combined sources19
Beta strandi107 – 110Combined sources4
Beta strandi116 – 123Combined sources8
Beta strandi125 – 130Combined sources6
Helixi134 – 136Combined sources3
Helixi139 – 152Combined sources14
Beta strandi155 – 160Combined sources6
Helixi164 – 166Combined sources3
Helixi170 – 178Combined sources9
Beta strandi183 – 186Combined sources4
Helixi189 – 198Combined sources10
Beta strandi201 – 203Combined sources3
Beta strandi207 – 210Combined sources4
Helixi215 – 224Combined sources10
Beta strandi228 – 230Combined sources3
Beta strandi238 – 243Combined sources6
Beta strandi245 – 247Combined sources3
Helixi249 – 260Combined sources12
Beta strandi267 – 273Combined sources7
Helixi275 – 291Combined sources17
Helixi296 – 305Combined sources10
Beta strandi307 – 310Combined sources4
Helixi314 – 324Combined sources11
Beta strandi327 – 333Combined sources7
Helixi336 – 338Combined sources3
Turni339 – 342Combined sources4
Beta strandi347 – 352Combined sources6
Helixi357 – 362Combined sources6
Beta strandi364 – 366Combined sources3
Helixi375 – 377Combined sources3
Helixi384 – 387Combined sources4
Beta strandi388 – 395Combined sources8
Helixi398 – 414Combined sources17
Helixi418 – 430Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G07X-ray1.95A1-430[»]
4G09X-ray1.90A1-430[»]
ProteinModelPortaliQ8G2R2.
SMRiQ8G2R2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G07X-ray1.95A1-430[»]
4G09X-ray1.90A1-430[»]
ProteinModelPortaliQ8G2R2.
SMRiQ8G2R2.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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

HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Miscellaneous databases

PROiQ8G2R2.

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_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: November 2, 2016
This is version 96 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

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.