SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

E3PRJ4

- KAMED_CLOSD

UniProt

E3PRJ4 - KAMED_CLOSD

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
D-lysine 5,6-aminomutase beta subunit
Gene
kamE, CLOST_1378
Organism
Clostridium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIB 10654)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the 1,2-migration of the D-lysine epsilon amino group to the delta carbon with concomitant reverse migration of a hydrogen atom to produce 2,5-diaminohexanoic acid.1 Publication

Catalytic activityi

D-lysine = 2,5-diaminohexanoate.1 Publication

Cofactori

Adenosylcobalamin.2 Publications
Pyridoxal phosphate.2 Publications

Enzyme regulationi

Rapidly inactivated in the presence of D-lysine and to a lesser extent in the absence of adenosylcobalamin (Adocbl). Activity is stable in the presence of Adocbl when D-lysine is absent. Adocbl imparts thermal stability at 37 degrees Celsius.1 Publication

Kineticsi

  1. KM=6.6 µM for adenosylcobalamin (for recombinant alpha and beta subunits expressed together in E.coli to overcome presence of corrinoids in native system)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi133 – 1331Cobalt (adenosylcobalamin axial ligand); via tele nitrogen

GO - Molecular functioni

  1. D-lysine 5,6-aminomutase activity Source: UniProtKB-EC
  2. cobalamin binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciCSTI499177:GJE9-1427-MONOMER.
UniPathwayiUPA00225.

Names & Taxonomyi

Protein namesi
Recommended name:
D-lysine 5,6-aminomutase beta subunit (EC:5.4.3.4)
Short name:
5,6-LAM
Gene namesi
Name:kamE
Ordered Locus Names:CLOST_1378
OrganismiClostridium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIB 10654)
Taxonomic identifieri499177 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium
ProteomesiUP000007041: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262D-lysine 5,6-aminomutase beta subunit
PRO_0000416984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441N6-(pyridoxal phosphate)lysine1 Publication

Interactioni

Subunit structurei

Heterotetramer of 2 alpha and 2 beta subunits.1 Publication

Protein-protein interaction databases

IntActiE3PRJ4. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 429
Helixi46 – 5712
Beta strandi65 – 739
Beta strandi76 – 838
Helixi106 – 11611
Beta strandi121 – 1288
Helixi135 – 1417
Helixi152 – 1543
Beta strandi158 – 1625
Beta strandi165 – 1673
Helixi169 – 17810
Beta strandi182 – 1876
Helixi195 – 20915
Helixi213 – 2153
Beta strandi216 – 2216
Helixi227 – 2315
Turni232 – 2343
Beta strandi236 – 2394
Helixi245 – 26016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XRSX-ray2.80B1-262[»]
ProteinModelPortaliE3PRJ4.
SMRiE3PRJ4. Positions 33-261.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini120 – 262143B12-binding
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 1367Adenosylcobalamin binding1 Publication
Regioni185 – 1928Adenosylcobalamin binding1 Publication
Regioni219 – 2235Adenosylcobalamin binding1 Publication
Regioni239 – 2446Adenosylcobalamin binding1 Publication

Sequence similaritiesi

Belongs to the KamE family.
Contains 1 B12-binding domain.

Phylogenomic databases

HOGENOMiHOG000223896.
KOiK18011.
OMAiPYGDRRD.

Family and domain databases

Gene3Di3.30.30.60. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR006158. Cobalamin-bd.
IPR028991. KamE_N.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
[Graphical view]
SUPFAMiSSF117778. SSF117778. 1 hit.
SSF52242. SSF52242. 1 hit.
PROSITEiPS51332. B12_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E3PRJ4-1 [UniParc]FASTAAdd to Basket

« Hide

MSSGLYSMEK KEFDKVLDLE RVKPYGDTMN DGKVQLSFTL PLKNNERSAE    50
AAKQIALKMG LEEPSVVMQQ SLDEEFTFFV VYGNFVQSVN YNEIHVEAVN 100
SEILSMEETD EYIKENIGRK IVVVGASTGT DAHTVGIDAI MNMKGYAGHY 150
GLERYEMIDA YNLGSQVANE DFIKKAVELE ADVLLVSQTV TQKNVHIQNM 200
THLIELLEAE GLRDRFVLLC GGPRINNEIA KELGYDAGFG PGRFADDVAT 250
FAVKTLNDRM NS 262
Length:262
Mass (Da):29,224
Last modified:March 8, 2011 - v1
Checksum:i248765160F6EF46F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104259 Genomic DNA. Translation: AAC79718.1.
FP565809 Genomic DNA. Translation: CBH21498.1.
RefSeqiYP_003936403.1. NC_014614.1.

Genome annotation databases

EnsemblBacteriaiCBH21498; CBH21498; CLOST_1378.
GeneIDi9854875.
KEGGicst:CLOST_1378.
PATRICi42273391. VBICloSti32817_1367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104259 Genomic DNA. Translation: AAC79718.1 .
FP565809 Genomic DNA. Translation: CBH21498.1 .
RefSeqi YP_003936403.1. NC_014614.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XRS X-ray 2.80 B 1-262 [» ]
ProteinModelPortali E3PRJ4.
SMRi E3PRJ4. Positions 33-261.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi E3PRJ4. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CBH21498 ; CBH21498 ; CLOST_1378 .
GeneIDi 9854875.
KEGGi cst:CLOST_1378.
PATRICi 42273391. VBICloSti32817_1367.

Phylogenomic databases

HOGENOMi HOG000223896.
KOi K18011.
OMAi PYGDRRD.

Enzyme and pathway databases

UniPathwayi UPA00225 .
BioCyci CSTI499177:GJE9-1427-MONOMER.

Family and domain databases

Gene3Di 3.30.30.60. 1 hit.
3.40.50.280. 1 hit.
InterProi IPR006158. Cobalamin-bd.
IPR028991. KamE_N.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
[Graphical view ]
SUPFAMi SSF117778. SSF117778. 1 hit.
SSF52242. SSF52242. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii."
    Chang C.H., Frey P.A.
    J. Biol. Chem. 275:106-114(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, EPR SPECTROSCOPY, PATHWAY.
  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. "A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase."
    Berkovitch F., Behshad E., Tang K.H., Enns E.A., Frey P.A., Drennan C.L.
    Proc. Natl. Acad. Sci. U.S.A. 101:15870-15875(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH B12 AND PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiKAMED_CLOSD
AccessioniPrimary (citable) accession number: E3PRJ4
Secondary accession number(s): Q9ZFE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: March 8, 2011
Last modified: September 3, 2014
This is version 22 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi