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P06988

- HISX_ECOLI

UniProt

P06988 - HISX_ECOLI

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 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.

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301NAD
Binding sitei188 – 1881NAD
Binding sitei211 – 2111NAD
Binding sitei237 – 2371Substrate
Metal bindingi259 – 2591Zinc
Binding sitei259 – 2591Substrate
Metal bindingi262 – 2621Zinc
Binding sitei262 – 2621Substrate
Active sitei326 – 3261Proton acceptor
Active sitei327 – 3271Proton acceptor
Binding sitei327 – 3271Substrate
Metal bindingi360 – 3601Zinc
Binding sitei360 – 3601Substrate
Binding sitei414 – 4141Substrate
Metal bindingi419 – 4191Zinc
Binding sitei419 – 4191Substrate

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: EcoCyc
  2. manganese ion binding Source: EcoCyc
  3. metal ion binding Source: EcoCyc
  4. NAD binding Source: InterPro
  5. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: EcoCyc
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

BioCyciEcoCyc:HISTDEHYD-MONOMER.
ECOL316407:JW2002-MONOMER.
MetaCyc:HISTDEHYD-MONOMER.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:hisD
Ordered Locus Names:b2020, JW2002
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10447. hisD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 434433Histidinol dehydrogenasePRO_0000135770Add
BLAST

Proteomic databases

PaxDbiP06988.
PRIDEiP06988.

2D gel databases

SWISS-2DPAGEP06988.

Expressioni

Gene expression databases

GenevestigatoriP06988.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP06988. 7 interactions.
STRINGi511145.b2020.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Helixi9 – 113Combined sources
Helixi14 – 207Combined sources
Helixi30 – 5425Combined sources
Beta strandi57 – 593Combined sources
Beta strandi64 – 674Combined sources
Helixi70 – 7910Combined sources
Helixi82 – 10019Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi115 – 1239Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi134 – 1363Combined sources
Helixi140 – 15213Combined sources
Beta strandi155 – 1617Combined sources
Helixi167 – 1759Combined sources
Beta strandi180 – 1834Combined sources
Helixi186 – 19510Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi204 – 2074Combined sources
Helixi212 – 22312Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi238 – 2436Combined sources
Helixi249 – 26012Combined sources
Beta strandi267 – 2737Combined sources
Helixi275 – 28915Combined sources
Helixi295 – 3028Combined sources
Beta strandi306 – 3094Combined sources
Helixi313 – 32311Combined sources
Beta strandi326 – 3327Combined sources
Helixi335 – 3384Combined sources
Helixi339 – 3413Combined sources
Beta strandi346 – 3516Combined sources
Helixi356 – 3616Combined sources
Beta strandi363 – 3653Combined sources
Helixi374 – 3763Combined sources
Helixi383 – 3864Combined sources
Beta strandi387 – 3959Combined sources
Helixi397 – 41317Combined sources
Helixi417 – 43317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K75X-ray1.75A/B1-434[»]
1KAEX-ray1.70A/B1-434[»]
1KAHX-ray2.10A/B1-434[»]
1KARX-ray2.10A/B1-434[»]
ProteinModelPortaliP06988.
SMRiP06988. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06988.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiP06988.
KOiK00013.
OMAiYAAKLCG.
OrthoDBiEOG6CVVCR.
PhylomeDBiP06988.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06988-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFNTIIDWN SCTAEQQRQL LMRPAISASE SITRTVNDIL DNVKARGDEA
60 70 80 90 100
LREYSAKFDK TTVTALKVSA EEIAAASERL SDELKQAMAV AVKNIETFHT
110 120 130 140 150
AQKLPPVDVE TQPGVRCQQV TRPVASVGLY IPGGSAPLFS TVLMLATPAS
160 170 180 190 200
IAGCKKVVLC SPPPIADEIL YAAQLCGVQD VFNVGGAQAI AALAFGTESV
210 220 230 240 250
PKVDKIFGPG NAFVTEAKRQ VSQRLDGAAI DMPAGPSEVL VIADSGATPD
260 270 280 290 300
FVASDLLSQA EHGPDSQVIL LTPAADMARR VAEAVERQLA ELPRAETARQ
310 320 330 340 350
ALNASRLIVT KDLAQCVEIS NQYGPEHLII QTRNARELVD SITSAGSVFL
360 370 380 390 400
GDWSPESAGD YASGTNHVLP TYGYTATCSS LGLADFQKRM TVQELSKEGF
410 420 430
SALASTIETL AAAERLTAHK NAVTLRVNAL KEQA
Length:434
Mass (Da):46,110
Last modified:January 23, 2007 - v5
Checksum:i4B4F2EA00C9BEA4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151E → V(PubMed:3062174)Curated
Sequence conflicti15 – 151E → V(PubMed:3018428)Curated
Sequence conflicti22 – 221M → T in CAA27610. (PubMed:3018428)Curated
Sequence conflicti150 – 1501S → R(PubMed:3062174)Curated
Sequence conflicti150 – 1501S → R(PubMed:3018428)Curated
Sequence conflicti157 – 1571V → A in CAA36882. (PubMed:2194167)Curated
Sequence conflicti313 – 3131L → S(PubMed:3062174)Curated
Sequence conflicti313 – 3131L → S(PubMed:3018428)Curated
Sequence conflicti403 – 4031L → V(PubMed:3062174)Curated
Sequence conflicti403 – 4031L → V(PubMed:3018428)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31812.1.
X03972 Genomic DNA. Translation: CAA27610.1.
X52656 Genomic DNA. Translation: CAA36882.1.
U00096 Genomic DNA. Translation: AAC75081.1.
AP009048 Genomic DNA. Translation: BAA15851.1.
M10483 Genomic DNA. Translation: AAA23962.1.
PIRiC64967. DEECHT.
RefSeqiNP_416524.1. NC_000913.3.
YP_490263.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75081; AAC75081; b2020.
BAA15851; BAA15851; BAA15851.
GeneIDi12931409.
946531.
KEGGiecj:Y75_p1983.
eco:b2020.
PATRICi32119375. VBIEscCol129921_2097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31812.1 .
X03972 Genomic DNA. Translation: CAA27610.1 .
X52656 Genomic DNA. Translation: CAA36882.1 .
U00096 Genomic DNA. Translation: AAC75081.1 .
AP009048 Genomic DNA. Translation: BAA15851.1 .
M10483 Genomic DNA. Translation: AAA23962.1 .
PIRi C64967. DEECHT.
RefSeqi NP_416524.1. NC_000913.3.
YP_490263.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K75 X-ray 1.75 A/B 1-434 [» ]
1KAE X-ray 1.70 A/B 1-434 [» ]
1KAH X-ray 2.10 A/B 1-434 [» ]
1KAR X-ray 2.10 A/B 1-434 [» ]
ProteinModelPortali P06988.
SMRi P06988. Positions 1-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P06988. 7 interactions.
STRINGi 511145.b2020.

Chemistry

ChEMBLi CHEMBL2366464.

2D gel databases

SWISS-2DPAGE P06988.

Proteomic databases

PaxDbi P06988.
PRIDEi P06988.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75081 ; AAC75081 ; b2020 .
BAA15851 ; BAA15851 ; BAA15851 .
GeneIDi 12931409.
946531.
KEGGi ecj:Y75_p1983.
eco:b2020.
PATRICi 32119375. VBIEscCol129921_2097.

Organism-specific databases

EchoBASEi EB0442.
EcoGenei EG10447. hisD.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
InParanoidi P06988.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.
PhylomeDBi P06988.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci EcoCyc:HISTDEHYD-MONOMER.
ECOL316407:JW2002-MONOMER.
MetaCyc:HISTDEHYD-MONOMER.

Miscellaneous databases

EvolutionaryTracei P06988.
PROi P06988.

Gene expression databases

Genevestigatori P06988.

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."
    Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.
    J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the Escherichia coli hisD gene and of the Escherichia coli and Salmonella typhimurium hisIE region."
    Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.
    Mol. Gen. Genet. 203:382-388(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide and amino acid polymorphism in the gene for L-histidinol dehydrogenase of Escherichia coli K12."
    Savic D.J., Jovanovic G., Kostic T.
    Nucleic Acids Res. 18:3634-3634(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3100 / ATCC 14948 / DSM 6302.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors."
    Bruni C.B., Musti A.M., Frunzio R., Blasi F.
    J. Bacteriol. 142:32-42(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-319.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  9. "Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase."
    Barbosa J.A.R.G., Sivaraman J., Li Y., Larocque R., Matte A., Schrag J.D., Cygler M.
    Proc. Natl. Acad. Sci. U.S.A. 99:1859-1864(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

Entry informationi

Entry nameiHISX_ECOLI
AccessioniPrimary (citable) accession number: P06988
Secondary accession number(s): O08506, P78076, Q47254
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 148 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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