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C4K4C4 (ALR_HAMD5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. HAMAP-Rule MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Alanine racemase HAMAP-Rule MF_01201
PRO_1000213835

Sites

Active site341Proton acceptor; specific for D-alanine By similarity
Active site2541Proton acceptor; specific for L-alanine By similarity
Binding site1291Substrate By similarity
Binding site3021Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue341N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C4K4C4 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 00ED6051FA0C5F9A

FASTA35839,378
        10         20         30         40         50         60 
MKGATAIINL KSLRHNLEKI QQYAPKSRLM AVVKANAYGH GLLTVAQALK NADYFSVARI 

        70         80         90        100        110        120 
EEALTLRSGG IIKPILLLEG FFSLEDLAVL QVNHIETVIH NFEQLVALEK VRLPEPVRVW 

       130        140        150        160        170        180 
MKIDTGMHRL GVRLEQADAF YQRLQNCPNV AKPIHIITHL SDVNPHHPVV TDQQIRSFDA 

       190        200        210        220        230        240 
FVQGKPGQKS IAASGAILLC PQSHRDVVRP GIALYGISPF EHFIGRDYGL LPVMTLQSPL 

       250        260        270        280        290        300 
IAVREHKAGE TVGYAGEWIS QTATFLGVLA IGYGDGYPQS APTGTPVWIN DRQVPIVGRV 

       310        320        330        340        350 
SMDMISVDLG RDATDKVGDR AVLWGDQLSL EKVASYIGYT AYELVSKLTG RVAISYVN 

« Hide

References

[1]"Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors."
Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.
Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5AT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001277 Genomic DNA. Translation: ACQ67417.1.
RefSeqYP_002923565.1. NC_012751.1.

3D structure databases

ProteinModelPortalC4K4C4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING572265.HDEF_0679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ67417; ACQ67417; HDEF_0679.
GeneID7950282.
KEGGhde:HDEF_0679.
PATRIC31972809. VBICanHam112931_0691.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
KOK01775.
OMALWQLEAI.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycHDEF572265:GJAB-684-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
3.20.20.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
IPR029066. PLP-binding_barrel.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SMARTSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_HAMD5
AccessionPrimary (citable) accession number: C4K4C4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: June 11, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways