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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Staphylococcus aureus (strain MRSA252)
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

Pathway: 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. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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 sitei119 – 1191NADUniRule annotation
Binding sitei180 – 1801NADUniRule annotation
Binding sitei203 – 2031NADUniRule annotation
Binding sitei226 – 2261SubstrateUniRule annotation
Metal bindingi248 – 2481ZincUniRule annotation
Binding sitei248 – 2481SubstrateUniRule annotation
Metal bindingi251 – 2511ZincUniRule annotation
Binding sitei251 – 2511SubstrateUniRule annotation
Active sitei316 – 3161Proton acceptorUniRule annotation
Active sitei317 – 3171Proton acceptorUniRule annotation
Binding sitei317 – 3171SubstrateUniRule annotation
Metal bindingi350 – 3501ZincUniRule annotation
Binding sitei350 – 3501SubstrateUniRule annotation
Binding sitei404 – 4041SubstrateUniRule annotation
Metal bindingi409 – 4091ZincUniRule annotation
Binding sitei409 – 4091SubstrateUniRule 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

BioCyciSAUR282458:GJA5-2798-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:SAR2760
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Histidinol dehydrogenasePRO_0000135850Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6GDC6.
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.

Q6GDC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPMLNAQQFL NQFSLEAPLD ESLYPIIRDI CQEVKVHGDK ALKMYNLTFD
60 70 80 90 100
HTKTDHLEIS HEQIKAAFDT LDEKTKQALQ QSYERIKAYQ ESIKQMNQQL
110 120 130 140 150
EESVECYEIY HPLESVGIYV PGGKASYPST VLMTATLAQV AGVENIVVVT
160 170 180 190 200
PPQPNGVSQE VLAACYITQV NQVFQVGGAQ SIAALTYGTE TIPKVDKIVG
210 220 230 240 250
PGNQFVAYAK KYLFGQVGID QIAGPTEIAL IIDDTADLDA IVYDVFAQAE
260 270 280 290 300
HDELARTYVI SEDAQVLKDL ESRIAKALPN VDRYDIVSKS IANQHYLIHA
310 320 330 340 350
SNFDEACHVM NTIAPEHASI QTVNPQPYIE KVKYVGALFI GHYSPEVIGD
360 370 380 390 400
YVAGPSHVLP TNRTARFTNG LSVNDFLTRN TVIHLSKDTF DQIADSAQHI
410
AHVEALYNHQ QSILIRQS
Length:418
Mass (Da):46,435
Last modified:July 19, 2004 - v1
Checksum:i519DCD4181C2EB61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG41735.1.
RefSeqiWP_001793834.1. NC_002952.2.
YP_042097.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG41735; CAG41735; SAR2760.
KEGGisar:SAR2760.
PATRICi19549236. VBIStaAur71814_2796.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG41735.1.
RefSeqiWP_001793834.1. NC_002952.2.
YP_042097.1. NC_002952.2.

3D structure databases

ProteinModelPortaliQ6GDC6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG41735; CAG41735; SAR2760.
KEGGisar:SAR2760.
PATRICi19549236. VBIStaAur71814_2796.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciSAUR282458:GJA5-2798-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: MRSA252.

Entry informationi

Entry nameiHISX_STAAR
AccessioniPrimary (citable) accession number: Q6GDC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 19, 2004
Last modified: June 24, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.