L-phenylalanine dehydrogenase - Rhodococcus sp.

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Unreviewed, UniProtKB/TrEMBL Q59771 (Q59771_RHOSO)

Last modified June 16, 2009. Version 48. History...

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Names and origin · Protein attributes · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Submitted name:
L-phenylalanine dehydrogenase EMBL AAA21461.1
EC=1.4.1.20

Gene names

Name:

pdh EMBL AAA21461.1

Organism

Rhodococcus sp. EMBL AAA21461.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Keywords
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	amino acid metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro phenylalanine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

355

L-phenylalanine dehydrogenase EMBL AAA21461.1

PRO_5000144128

Sequences

Sequence

Length

Mass (Da)

Tools

Q59771-1 [UniParc].

Last modified December 1, 2001. Version 2.
Checksum: A969C29E9466935E
Show »

356

36,609

        10         20         30         40         50         60 
MSIDSALNWD GEMTVTRFDR ETGAHFVIRL DSTQLGPAAG GTRAAQYSQL ADALTDAGKL 

        70         80         90        100        110        120 
AGAMTLKMAV SNLPMGGGKS VIALPAPRHS IDPSTWARIL RIHAENIDKL SGNYWTGPDV 

       130        140        150        160        170        180 
NTNSADMDTL NDTTEFVFGR SLERGGAGSS AFTTAVGVFE AMKATVAHRG LGSLDGLTVL 

       190        200        210        220        230        240 
VQGLGAVGGS LASLAAEAGA QLLVADTDTE RVAHAVALGH TAVALEDVLS TPCDVFAPCA 

       250        260        270        280        290        300 
MGGVITTEVA RTLDCSVVAG AANNVIADEA ASDILHARGI LYAPDFVANA GGAIHLVGRE 

       310        320        330        340        350 
VLGWSESVVH ERAVAIGDTL NQVFEISDND GVTPDEAART LAGRRAREAS TTTATA

References

[1]	"Cloning, sequencing, and expression of Rhodococcus L-phenylalanine dehydrogenase. Sequence comparisons to amino-acid dehydrogenases." Brunhuber N.M., Banerjee A., Jacobs W.R. Jr, Blanchard J.S. J. Biol. Chem. 269:16203-16211(1994) [PubMed: 8206922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: M4 EMBL AAA21461.1.
[2]	"Purification, characterization, and kinetic mechanism of L-phenylalanine dehydrogenase." Brunhuber N.M.W., Hummel W., Blanchard J.S. Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: M4 EMBL AAA21461.1.
[3]	"Phenylalanine dehydrogenase from Rhodococcus sp. M4: high-resolution X-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism." Vanhooke J.L., Thoden J.B., Brunhuber N.M., Blanchard J.S., Holden H.M. Biochemistry 38:2326-2339(1999) [PubMed: 10029526] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[4]	"Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity." Brunhuber N.M., Thoden J.B., Blanchard J.S., Vanhooke J.L. Biochemistry 39:9174-9187(2000) [PubMed: 10924111] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-356.

Cross-references

Sequence databases

U08381 Genomic DNA. Translation: AAA21461.1.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BW9	X-ray	1.50	A	1-356	[»]
			B	1-356	[»]
1BXG	X-ray	2.30	A	1-356	[»]
			B	1-356	[»]
1C1D	X-ray	1.25	A	2-356	[»]
			B	2-356	[»]
1C1X	X-ray	1.40	A	2-356	[»]
			B	2-356	[»]

ModBase

Family and domain databases

InterPro

IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer.
IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000188. Phe_leu_dh. 1 hit.

PRINTS

PR00082. GLFDHDRGNASE.

ProtoNet

Entry information

Entry name

Q59771_RHOSO

Accession

Primary (citable) accession number: Q59771

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information