Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7N6I1 (HIS8_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative histidine biosynthesis bifunctional protein HisCD

Including the following 2 domains:

  1. Histidinol dehydrogenase
    Short name=HDH
    EC=1.1.1.23
  2. Histidinol-phosphate aminotransferase
    EC=2.6.1.9
    Alternative name(s):
    Imidazole acetol-phosphate transaminase
Gene names
Name:hisCD
Synonyms:hisD
Ordered Locus Names:plu1569
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length807 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01023

Catalytic activity

L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP-Rule MF_01023

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01023

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01023

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01023

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP-Rule MF_01023

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01023

Sequence similarities

In the N-terminal section; belongs to the histidinol dehydrogenase family.

In the C-terminal section; belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 807807Putative histidine biosynthesis bifunctional protein HisCD HAMAP-Rule MF_01023
PRO_0000153415

Regions

Region1 – 440440Histidinol dehydrogenase HAMAP-Rule MF_01023
Region441 – 807367Histidinol-phosphate aminotransferase HAMAP-Rule MF_01023

Sites

Active site3281 By similarity
Active site3291 By similarity
Metal binding2611Zinc By similarity
Metal binding2641Zinc By similarity
Metal binding3621Zinc By similarity
Metal binding4211Zinc By similarity

Amino acid modifications

Modified residue6551N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N6I1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 648F98DD2F9F706E

FASTA80788,850
        10         20         30         40         50         60 
MTDHFDTLIR WQECHDEQQN ALLTRPAISA SVEISRTVEQ ILHAVKEYGD HTLREFSRRF 

        70         80         90        100        110        120 
DKTVIENIRI SPEEIAAAEN SLNNDIKQAM QQAMNNIRVF HEAQKPIKIE VETQPGVYCQ 

       130        140        150        160        170        180 
QVTRPIDSVG LYIPGGSAPL LSTVLMLGTP AQIAGCHKVV LCSPPPIANE ILYAATLCGI 

       190        200        210        220        230        240 
TEIFQIGGAQ AIAAMAFGTE SVPKVDKIFG PGNAYVTEAK RQVSQRVDGA TIDMPAGPSE 

       250        260        270        280        290        300 
LLIIADAGAN PVFVAADLLS QAEHGPDSQV ILVTPDEALA KKVITEIEKQ LTRLPRNQIA 

       310        320        330        340        350        360 
AKALAHSRII VTTSLQQCVE ISNRYGPEHL IIQTRQPEQL VEKITSAGSV FLGDWSPESA 

       370        380        390        400        410        420 
GDYASGTNHV LPTYGYTSTY SSLGLADFLK RMTIQQLTPQ GLLNLSQTIE TLAQAEQLTA 

       430        440        450        460        470        480 
HKNALTLRVA ALNIAGQGVN MNNIFDANLL ARENIRKLTP YMSARRLGGK GDVWLNANEY 

       490        500        510        520        530        540 
PLAPDFQCTE QTLNRYPDCQ PASVIRRYAA YAGLQPEQVL ACRGADESIE LLIRVFCEPG 

       550        560        570        580        590        600 
QDVVLFCPPT YGMYSVSAET FGVEQKKITA LENWQLDIEA IENNLDRVKL IYICSPNNPT 

       610        620        630        640        650        660 
GNAINPDSLR KILELTANRA IVTIDEAYIE FCPENSIASW LKNYPNLVIL RTLSKAFALA 

       670        680        690        700        710        720 
GLRCGFTLAS VDIITLLLKV IAPYPLSTPV ADIAAQALTA ENIAIMQKRV VEIRENRNDL 

       730        740        750        760        770        780 
QQALNKLAIV EKVFPSETNY ILVKFYDAET VFKTLWHQGI ILRDQRKQPG LEGCLRITIG 

       790        800 
SRKECERVVE AISALSTVNE QPKEIAN 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571864 Genomic DNA. Translation: CAE13862.1.
RefSeqNP_928860.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N6I1.
SMRQ7N6I1. Positions 5-432, 450-794.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243265.plu1569.

Proteomic databases

PRIDEQ7N6I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE13862; CAE13862; plu1569.
GeneID2801564.
KEGGplu:plu1569.
PATRIC20507017. VBIPhoLum48522_1751.

Organism-specific databases

GenoListplu1569.
CMRSearch...

Phylogenomic databases

eggNOGCOG0079.
KOK00013.
OMASSEWITA.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

UniPathwayUPA00031; UER00012.
UPA00031; UER00014.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01023. HisC_aminotrans_2.
MF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
PF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53383. SSF53383. 1 hit.
SSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01141. hisC. 1 hit.
TIGR00069. hisD. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS8_PHOLL
AccessionPrimary (citable) accession number: Q7N6I1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways