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A1U388 (ALR_MARAV) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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 length357 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 – 357357Alanine racemase HAMAP-Rule MF_01201
PRO_1000066008

Sites

Active site351Proton acceptor; specific for D-alanine By similarity
Active site2541Proton acceptor; specific for L-alanine By similarity
Binding site1281Substrate By similarity
Binding site3021Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1U388 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F4DEE09F3350C735

FASTA35738,607
        10         20         30         40         50         60 
MPRPTVARID LDALKHNFRR ARELAGTAYA MAVVKADGYG HGIRSVADAL APETSRFAVA 

        70         80         90        100        110        120 
CIEEAIAIRG AGHRHSVVLL QGTHQKDDLA ECERSGFEPV LHCQQQLSWL GAGRSPRFWI 

       130        140        150        160        170        180 
KVNTGMNRLG FRPEELPEVM AGLEEAGLKH LAIGFVTHFA CADDSDSEMT GLQTRIFERA 

       190        200        210        220        230        240 
VAPWPDLMRS VGNSAAHFRP NQPLYEWSRP GIMLYGASPM EGKTGAELGL CPAMTLQAPL 

       250        260        270        280        290        300 
ITTRVVRAGE SVGYGASWTA SQDTRMGMVA IGYADGYPRH AGTGTPAAVR GQRIRLLGRV 

       310        320        330        340        350 
SMDMLAVDLS AVPEAREGDM VELWGKTVSV DEVATCAGTI GYELLTGVTS RVPRVHE 

« Hide

References

[1]"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000514 Genomic DNA. Translation: ABM19457.1.
RefSeqYP_959644.1. NC_008740.1.

3D structure databases

ProteinModelPortalA1U388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351348.Maqu_2381.

Proteomic databases

PRIDEA1U388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM19457; ABM19457; Maqu_2381.
GeneID4656656.
KEGGmaq:Maqu_2381.
PATRIC22460092. VBIMarAqu65105_2796.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMATRIAIMA.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycMHYD351348:GHYZ-2431-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_MARAV
AccessionPrimary (citable) accession number: A1U388
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 58 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