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A9AHS1 (A9AHS1_BURM1) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length356 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. SAAS SAAS009006 HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS009006 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. RuleBase RU004188 HAMAP-Rule MF_01201

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site351Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2531Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1301Substrate By similarity HAMAP-Rule MF_01201
Binding site3011Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
A9AHS1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 3E7C2B87E2C6A1F2

FASTA35638,105
        10         20         30         40         50         60 
MPRPISATIH TAALANNLSV VRRYAGPSKV WAVVKANAYG HGLARVFPGL RGTDGFGLLD 

        70         80         90        100        110        120 
LDEAVKLREL GWAGPILLLE GFFRSTDIDV IDRYSLTTTV HNDEQMRMLE TARLSKPVNV 

       130        140        150        160        170        180 
QLKMNSGMNR LGYAPEKYRA AWERARACPS IGQITLMTHF SDADNERGVA EQLATFERGA 

       190        200        210        220        230        240 
ANIAGARCLA NSAAVLWHPD THFDWVRPGI VLYGASPSGL SSDIADTGLK PAMTLSSELI 

       250        260        270        280        290        300 
AVQSIGKGQA IGYGSTFSAP APMRIGVVAC GYADGYPRVA PEGTPVIVDG IRTRIVGRVS 

       310        320        330        340        350 
MDMITVDLTP CPQAGVGARV ELWGNALSID DVARHCGTIG YELMCAVAAR VPVRAE 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Burkholderia multivorans ATCC 17616."
Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 EMBL BAG43926.1 and ATCC 17616 / 249.
[2]"Complete sequence of chromosome 1 of Burkholderia multivorans ATCC 17616."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 / 249.
[3]"Complete sequence of chromosome1 of Burkholderia multivorans ATCC 17616."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 17616 EMBL ABX14926.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000868 Genomic DNA. Translation: ABX14926.1.
AP009385 Genomic DNA. Translation: BAG43926.1.
RefSeqYP_001579423.1. NC_010084.1.
YP_001946462.1. NC_010804.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395019.Bmul_1238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX14926; ABX14926; Bmul_1238.
BAG43926; BAG43926; BMULJ_02009.
GeneID5767054.
6360178.
KEGGbmj:BMULJ_02009.
bmu:Bmul_1238.
PATRIC19165853. VBIBurMul203716_2999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMARDLELCS.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycBMUL395019:GIYO-2007-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 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.
[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.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA9AHS1_BURM1
AccessionPrimary (citable) accession number: A9AHS1
Entry history
Integrated into UniProtKB/TrEMBL: January 15, 2008
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)