Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04NA9 (Q04NA9_LEPBJ) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 60. Feed History...

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

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 RuleBase RU004247 SAAS SAAS020622

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS020622

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. HAMAP-Rule MF_01201 RuleBase RU004188

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site381Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2711Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1341Substrate By similarity HAMAP-Rule MF_01201
Binding site3191Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue381N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
Q04NA9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 4838C83698448241

FASTA37942,066
        10         20         30         40         50         60 
MKETASSWIE ISKRSLSNNL NSFRSILRPG STLTAILKSN AYGHGTDLMA KLCIEEGVSH 

        70         80         90        100        110        120 
IGVNSIEEAQ SIRQIDPKIP ILIMGEIQNP EKRKEALSDP NFWIIFSRPE TARILSSLNP 

       130        140        150        160        170        180 
APKLHLKIDT GMGRLGNHGE TLKYTLGELK KNGITLDGIC THFASTEDVL EHKYSLMQIQ 

       190        200        210        220        230        240 
KFEKAVLLAE SLGYKNLIRH MCASASTMLF SSAHYEMVRV GISLYGLWPS IQTRLSLNLN 

       250        260        270        280        290        300 
GNKNFQLSPI LSWKTRIVHI QNHPADSYIG YGSTFQTSYP TKVAIVPIGY YEGLDRKLSS 

       310        320        330        340        350        360 
NGDMLVLGKR ARIIGRICMN MTMLDVTHIS GADVGSVVTV IGQDGEELIT ADDIADRTHT 

       370 
INYEITTRIS ESVCRIVVD 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197 EMBL ABJ77611.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000351 Genomic DNA. Translation: ABJ77611.1.
RefSeqYP_802369.1. NC_008511.1.

3D structure databases

ProteinModelPortalQ04NA9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355277.LBJ_4232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ77611; ABJ77611; LBJ_4232.
GeneID4412304.
KEGGlbj:LBJ_4232.
PATRIC22362959. VBILepBor13265_4162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAWRDMARR.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycLBOR355277:GHYM-3212-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 nameQ04NA9_LEPBJ
AccessionPrimary (citable) accession number: Q04NA9
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)