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F0N5D5 (F0N5D5_NEIMO) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length352 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 SAAS SAAS009006

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201 SAAS SAAS009006

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site331Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2501Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1291Substrate By similarity HAMAP-Rule MF_01201
Binding site2981Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue331N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
F0N5D5 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 8E4C3B318BAFF958

FASTA35238,845
        10         20         30         40         50         60 
MRPLNVQIRL GNLRHNYRIL KEMHGGKLLA VVKADAYGHG AVRCAFALAD LADGFAVATI 

        70         80         90        100        110        120 
DEGIRLRESG ITHPIVLLEG VFEASEYEAV EQYSLWPAVG NQWQLEALLI RHWKKPVKVW 

       130        140        150        160        170        180 
LKMDSGMHRT GFFPHDYASA YAALKQSEYV DSIVKFSHFS CADEPESGMT EIQMEAFDLG 

       190        200        210        220        230        240 
TKGLEGEESL ANSAAILNVP EARRDWGRAG LALYGISPFG GSDDRLKPVM RLSTRIFGER 

       250        260        270        280        290        300 
VLQPHSPIGY GATFYTSKST RVGLIACGYA DGYPRRAPSN SPVAVDGKLT RVIGRVSMDM 

       310        320        330        340        350 
MTIELDASQE GLGHEVELWG DTVNINTVAE AAGTIPYELM CNIKRAKFTY IE 

« Hide

References

[1]"Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination."
Budroni S., Siena E., Dunning Hotopp J.C., Seib K.L., Serruto D., Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.
Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M04-240196 EMBL ADZ01083.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002423 Genomic DNA. Translation: ADZ01083.1.
RefSeqYP_005897322.1. NC_017515.1.

3D structure databases

ProteinModelPortalF0N5D5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ01083; ADZ01083; NMBM04240196_0585.
GeneID12487647.
KEGGnmq:NMBM04240196_0585.
PATRIC47167652. VBINeiMen179694_0748.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01775.

Enzyme and pathway databases

BioCycNMEN935593:GLHT-584-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 nameF0N5D5_NEIMO
AccessionPrimary (citable) accession number: F0N5D5
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: February 19, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)