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B1Y2H6 (ALR_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. 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

Names and origin

Protein attributes

Sequence length377 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 – 377377Alanine racemase HAMAP-Rule MF_01201
PRO_1000138612

Sites

Active site351Proton acceptor; specific for D-alanine By similarity
Active site2601Proton acceptor; specific for L-alanine By similarity
Binding site1301Substrate By similarity
Binding site3121Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1Y2H6 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: A3226A32E785C400

FASTA37741,105
        10         20         30         40         50         60 
MPRPIEALIH PDALAHNLLQ ARRHAGDAKL WAVIKANAYG HGIERVWPAL LGADGLAMLD 

        70         80         90        100        110        120 
LDEAQRVRNL GWRGPVLLLE GCFEARDLEL CSRLNLWHVV HHDDQIGWLA AHKTHQPHRV 

       130        140        150        160        170        180 
FLKMNSGMNR LGFTPQALRS AWVRLNALPQ VDEISLMTHF SDADSPRPGA DGIAAQVARF 

       190        200        210        220        230        240 
VEATHDLPGE RSLSNSAAIL RHCERAEVRA DWVRSGILSY GSSPDHPQHD IGHWNLRPAM 

       250        260        270        280        290        300 
TLRSRLIATQ QLQAGDSVGY GSRFVAQQPM RIGIVACGYA DGYPRHAPGD TGNATPVLVD 

       310        320        330        340        350        360 
GLRTHTVGRV SMDMLAVDLS ELPAAGVGSE VTLWGHGPHG SLLPIDAVAQ AAGTIGYELM 

       370 
CALAQRVPTH VQDLEPR 

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001013 Genomic DNA. Translation: ACB33192.1.
RefSeqYP_001789957.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y2H6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395495.Lcho_0920.

Proteomic databases

PRIDEB1Y2H6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB33192; ACB33192; Lcho_0920.
GeneID6159901.
KEGGlch:Lcho_0920.
PATRIC22392117. VBILepCho83238_0919.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMAISHFACA.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycLCHO395495:GHYL-929-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_LEPCP
AccessionPrimary (citable) accession number: B1Y2H6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 48 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