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Protein

D-ornithine 4,5-aminomutase subunit alpha

Gene

oraS

Organism
Clostridium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIB 10654)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. The role of OraS remains obscure; however, it seems to be required for a correct folding of the OraE subunit. The complex is active only on D-ornithine and 2,4-diaminopentanoic acid and not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D-alpha-lysine.3 Publications

Catalytic activityi

D-ornithine = (2R,4S)-2,4-diaminopentanoate.3 Publications

Enzyme regulationi

Increased activity in the presence of dithiothreitol (DTT) in vitro. Inhibited by 1 mM potassium phosphate and potassium chloride. Inhibited by L-alpha-ornithine, D,L-alpha-lysine, L-beta-lysine (50%-60%), L-alpha-lysine (26%) and by delta-amino-n-valeric acid to a lesser extent. Significant decrease in activity is observed in the presence of 0.2 mM p-chloromercuribenzoate, N-ethylmaleimide and also by 2 mM iodoacetate to a lesser extent but not inhibited by arsenite.2 Publications

pH dependencei

Optimum pH is 9.0 or between 8.5-8.7 (with Tris-HCl buffer). Half-maximal activity is observed at pH 7.4 and 9.7.2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius for native enzyme. Displays half-maximal activity at 23 degrees Celsius and 49 degrees Celsius. Rapidly inactivated at temperatures above 45 degrees Celsius. Loses more than 35% and 30% of its activity when stored at -20 degrees Celsius for 1 month and at 4 degrees Celsius for 48 hours, respectively.2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciCSTI499177:GJE9-1339-MONOMER.
BRENDAi5.4.3.5. 1522.

Names & Taxonomyi

Protein namesi
Recommended name:
D-ornithine 4,5-aminomutase subunit alpha (EC:5.4.3.5Imported)
Alternative name(s):
D-ornithine aminomutase S component1 Publication
Short name:
OAM-S
Gene namesi
Name:oraS
Ordered Locus Names:CLOST_1291
OrganismiClostridium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIB 10654)
Taxonomic identifieri499177 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium
Proteomesi
  • UP000007041 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121121D-ornithine 4,5-aminomutase subunit alphaPRO_0000421804Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of 2 alpha (OraS) and 2 beta (OraE) subunits.3 Publications

Protein-protein interaction databases

STRINGi499177.CLOST_1291.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Helixi12 – 143Combined sources
Helixi19 – 4325Combined sources
Helixi47 – 5610Combined sources
Helixi61 – 7313Combined sources
Helixi77 – 793Combined sources
Helixi81 – 9111Combined sources
Helixi96 – 1049Combined sources
Helixi109 – 1135Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KOWX-ray2.90E/F/G/H1-121[»]
3KOXX-ray2.40E/F/G/H1-121[»]
3KOYX-ray2.80E/F/G/H1-121[»]
3KOZX-ray2.80E/F/G/H1-121[»]
3KP0X-ray2.80E/F/G/H1-121[»]
3KP1X-ray2.01E/F/G/H1-121[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiE3PY96.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105KIJ. Bacteria.
ENOG4111S56. LUCA.
HOGENOMiHOG000292272.
KOiK17899.
OMAiKRADDFQ.

Family and domain databases

InterProiIPR016176. Cbl-dep_enz_cat.
IPR015130. Lys-AminoMut_A.
[Graphical view]
PfamiPF16552. OAM_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF51703. SSF51703. 1 hit.

Sequencei

Sequence statusi: Complete.

E3PY96-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRADDFQQR RAHLANLSDE ELQTRFWEMA EKIVDPLLDL GKKNTTPSIE
60 70 80 90 100
RSVLLRMGFS SLEAKAIVDK TMDRGLMGKG AGHIVYKIAK EKNISVREAG
110 120
LALSEGKYWD DAIQIFKGGV K
Length:121
Mass (Da):13,623
Last modified:March 8, 2011 - v1
Checksum:i62D4FC5EA0087F86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY038595 Genomic DNA. Translation: AAK72501.1.
FP565809 Genomic DNA. Translation: CBH21411.1.

Genome annotation databases

EnsemblBacteriaiCBH21411; CBH21411; CLOST_1291.
KEGGicst:CLOST_1291.
PATRICi42273213. VBICloSti32817_1278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY038595 Genomic DNA. Translation: AAK72501.1.
FP565809 Genomic DNA. Translation: CBH21411.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KOWX-ray2.90E/F/G/H1-121[»]
3KOXX-ray2.40E/F/G/H1-121[»]
3KOYX-ray2.80E/F/G/H1-121[»]
3KOZX-ray2.80E/F/G/H1-121[»]
3KP0X-ray2.80E/F/G/H1-121[»]
3KP1X-ray2.01E/F/G/H1-121[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi499177.CLOST_1291.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBH21411; CBH21411; CLOST_1291.
KEGGicst:CLOST_1291.
PATRICi42273213. VBICloSti32817_1278.

Phylogenomic databases

eggNOGiENOG4105KIJ. Bacteria.
ENOG4111S56. LUCA.
HOGENOMiHOG000292272.
KOiK17899.
OMAiKRADDFQ.

Enzyme and pathway databases

BioCyciCSTI499177:GJE9-1339-MONOMER.
BRENDAi5.4.3.5. 1522.

Miscellaneous databases

EvolutionaryTraceiE3PY96.

Family and domain databases

InterProiIPR016176. Cbl-dep_enz_cat.
IPR015130. Lys-AminoMut_A.
[Graphical view]
PfamiPF16552. OAM_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF51703. SSF51703. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-ornithine aminomutase from Clostridium sticklandii."
    Chen H.P., Wu S.H., Lin Y.L., Chen C.M., Tsay S.S.
    J. Biol. Chem. 276:44744-44750(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    Strain: ATCC 12662 / DSM 519 / JCM 1433 / NCIB 106541 Publication.
  2. "Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence."
    Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R., Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M., Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.
    BMC Genomics 11:555-555(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12662 / DSM 519 / JCM 1433 / NCIB 10654.
  3. "Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D-ornithine 5,4-aminomutase."
    Somack R., Costilow R.N.
    Biochemistry 12:2597-2604(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 12662 / DSM 519 / JCM 1433 / NCIB 106541 Publication.
  4. "Amino mutases."
    Baker J.J., Stadtman T.C.
    (In) Dolphin D. (eds.); B12, pp.2:203-231, Wiley Interscience, New York (1982)
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  5. "Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase."
    Wolthers K.R., Levy C., Scrutton N.S., Leys D.
    J. Biol. Chem. 285:13942-13950(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH ORAE SUBUNIT, SUBUNIT.
    Strain: ATCC 12662 / DSM 519 / JCM 1433 / NCIB 106541 Publication.

Entry informationi

Entry nameiOAMS_CLOSD
AccessioniPrimary (citable) accession number: E3PY96
Secondary accession number(s): Q8VPJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 8, 2011
Last modified: November 11, 2015
This is version 25 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.