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

B9GH07 (B9GH07_POPTR) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 44. Feed History...

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

Names and origin

Protein attributes

Sequence length441 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. PIRNR PIRNR000099

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. PIRNR PIRNR000099

Cofactor

Binds 1 zinc ion per subunit By similarity. PIRSR PIRSR000099-4

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. PIRNR PIRNR000099

Subcellular location

Plastidchloroplast By similarity PIRNR PIRNR000099.

Sequence similarities

Belongs to the histidinol dehydrogenase family. RuleBase RU004175 PIRNR PIRNR000099

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site3281Proton acceptor By similarity PIRSR PIRSR000099-1
Active site3291Proton acceptor By similarity PIRSR PIRSR000099-1
Metal binding2601Zinc By similarity PIRSR PIRSR000099-4
Metal binding2631Zinc By similarity PIRSR PIRSR000099-4
Metal binding3621Zinc By similarity PIRSR PIRSR000099-4
Metal binding4211Zinc By similarity PIRSR PIRSR000099-4
Binding site1271NAD By similarity PIRSR PIRSR000099-2
Binding site1891NAD By similarity PIRSR PIRSR000099-2
Binding site2121NAD By similarity PIRSR PIRSR000099-2
Binding site2381Substrate By similarity
Binding site2601Substrate By similarity
Binding site2631Substrate By similarity
Binding site3291Substrate By similarity
Binding site3621Substrate By similarity
Binding site4161Substrate By similarity
Binding site4211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B9GH07 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: E10AFE0C50A7EAF6

FASTA44147,768
        10         20         30         40         50         60 
MCAMKSYRLS ELNNSEVESL KARPRIDFSS IFGIVNPIVD DVRQRGDAAV KDYTSRFDKV 

        70         80         90        100        110        120 
KLDKIVENVS ELPDPELDAT VKEAFDVAYN NIYAFHLAQK SVEKSVETMK GVRCKRVARS 

       130        140        150        160        170        180 
ISSVGLYVPG GTAVLPSTAL MLAIPAQIAG CKTVVLATPP AQDGSICKEV LYCAKKAGVT 

       190        200        210        220        230        240 
HILKAGGAQA ISAMAWGTES CPKAEKIFGP GNQYVTAAKM ILQNSEAMIS IDMPAGPSEV 

       250        260        270        280        290        300 
LVIADRYASP VHIAADLLSQ AEHGPDSQVV LVVAGDGVDM KAIEEEISKQ CQSLPRGEYA 

       310        320        330        340        350        360 
SKALSHSFTV FARDMVEAVS FSNLYAPEHL IINVKEAEKW ESFIENAGSV FLGPWTPESV 

       370        380        390        400        410        420 
GDYASGTNHV LPTYGYARMY GGVSLDSFQK YMTVQSLTEE GLRKLGPYVA TMAEVEGLDA 

       430        440 
HKRAVTLRLQ DIEARQVSNT R 

« Hide

References

« Hide 'large scale' references
[1]"The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."
Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., Brun A. expand/collapse author list , Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.
Science 313:1596-1604(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nisqually.
[2]US DOE Joint Genome Institute (JGI-PGF)
Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S., Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S., Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M. expand/collapse author list , Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B., Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D., Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J., Tuskan G., Rokhsar D.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Nisqually.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000337 Genomic DNA. Translation: EEE85368.1.
RefSeqXP_002300563.1. XM_002300527.2.

3D structure databases

ProteinModelPortalB9GH07.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3694.eugene3.00013048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsPOPTR_0001s46960.1; POPTR_0001s46960.1; POPTR_0001s46960.
GeneID7480422.
KEGGpop:POPTR_550607.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAERISSFH.
ProtClustDBPLN02926.

Enzyme and pathway databases

UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB9GH07_POPTR
AccessionPrimary (citable) accession number: B9GH07
Entry history
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)