B9GH07 (B9GH07_POPTR) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Predicted protein EMBL EEE85368.1

Gene names

ORF Names:

POPTRDRAFT_550607 EMBL EEE85368.1

Organism

Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) [Reference proteome]

Taxonomic identifier

3694 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Salicaceae › Saliceae › Populus

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Inferred 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	Plastid › chloroplast By similarity PIRNR PIRNR000099.
Sequence similarities	Belongs to the histidinol dehydrogenase family. RuleBase RU004175 PIRNR PIRNR000099

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis PIRNR PIRNR000099
Cellular component	Chloroplast PIRNR PIRNR000099 Plastid
Ligand	Metal-binding PIRSR PIRSR000099-4 NAD PIRSR PIRSR000099-2 PIRNR PIRNR000099 Zinc PIRSR PIRSR000099-4
Molecular function	Oxidoreductase PIRNR PIRNR000099
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway pollen development Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to UV Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Cellular_component	chloroplast stroma Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	328	1	Proton acceptor By similarity PIRSR PIRSR000099-1
	Active site	329	1	Proton acceptor By similarity PIRSR PIRSR000099-1
	Metal binding	260	1	Zinc By similarity PIRSR PIRSR000099-4
	Metal binding	263	1	Zinc By similarity PIRSR PIRSR000099-4
	Metal binding	362	1	Zinc By similarity PIRSR PIRSR000099-4
	Metal binding	421	1	Zinc By similarity PIRSR PIRSR000099-4
	Binding site	127	1	NAD By similarity PIRSR PIRSR000099-2
	Binding site	189	1	NAD By similarity PIRSR PIRSR000099-2
	Binding site	212	1	NAD By similarity PIRSR PIRSR000099-2
	Binding site	238	1	Substrate By similarity PIRSR PIRSR000099-3
	Binding site	260	1	Substrate By similarity PIRSR PIRSR000099-3
	Binding site	263	1	Substrate By similarity PIRSR PIRSR000099-3
	Binding site	329	1	Substrate By similarity PIRSR PIRSR000099-3
	Binding site	362	1	Substrate By similarity PIRSR PIRSR000099-3
	Binding site	416	1	Substrate By similarity PIRSR PIRSR000099-3
	Binding site	421	1	Substrate By similarity PIRSR PIRSR000099-3

Sequences

	Sequence		Length	Mass (Da)
	B9GH07 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: E10AFE0C50A7EAF6	FASTA	441	47,768
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
RefSeq	XP_002300563.1. XM_002300527.1.
UniGene	Pth.8892.
3D structure databases
ProteinModelPortal	B9GH07.
ModBase	Search...
Protein-protein interaction databases
STRING	3694.eugene3.00013048.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	POPTR_0001s46960.1; POPTR_0001s46960.1; POPTR_0001s46960.
GeneID	7480422.
KEGG	pop:POPTR_550607.
Phylogenomic databases
eggNOG	COG0141.
HOGENOM	HOG000243914.
KO	K00013.
OMA	GYAKNYS.
ProtClustDB	PLN02926.
Enzyme and pathway databases
UniPathway	UPA00031; UER00014.
Family and domain databases
HAMAP	MF_01024. HisD.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR001692. Histidinol_DH_CS. IPR022695. Histidinol_DH_monofunct. IPR012131. Hstdl_DH. [Graphical view]
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000099. Histidinol_dh. 1 hit.
PRINTS	PR00083. HOLDHDRGNASE.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00069. hisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B9GH07_POPTR

Accession

Primary (citable) accession number: B9GH07

Entry history

Integrated into UniProtKB/TrEMBL:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	April 3, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)