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

A6VH99 (A6VH99_METM7) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 46. 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

Names and origin

Protein attributes

Sequence length373 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. HAMAP-Rule MF_01201

Ontologies

Keywords
   LigandPyridoxal phosphate HAMAP-Rule MF_01201
   Molecular functionIsomerase HAMAP-Rule MF_01201 EMBL ABR65825.1
   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

Sites

Active site371Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2661Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site1351Substrate By similarity HAMAP-Rule MF_01201
Binding site3131Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue371N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
A6VH99 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: C8D190DB9A17872A

FASTA37341,788
        10         20         30         40         50         60 
MVSHPIWAEI DLSAIKNNIQ EIRRITNPKS QVMAVVKANA YGHGAIEVSK VCLENGADRL 

        70         80         90        100        110        120 
AVARSTEALE LRNAGITCPI LVFGYCTEEE IEKMVENDIT LTVYSFETAE SIQKIAEKLG 

       130        140        150        160        170        180 
KHSKIHIKVD TGMGRLGFLP KKEAIETIKK IMELKNIKIE GIYTHFADAD NSDKSYTTMQ 

       190        200        210        220        230        240 
FSRFTNFLHN LEENEIFIPI KHASNSAAII DHPETHLNLV RPGIILYGLY PSELVHKERI 

       250        260        270        280        290        300 
NLKPAMSLKV LITHVKEVPE NTKISYGCTF ETKKPSKIAS LPIGYADGFT RMLKDGYVLI 

       310        320        330        340        350        360 
HGSRVPVIGR ICMDQCMIDV SDIENVQVGD VVTIFGTQEN EKIPIEEFGE KLGTINYELV 

       370 
CMVAGRVPRK YLP 

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C7."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C7 / ATCC BAA-1331.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000745 Genomic DNA. Translation: ABR65825.1.
RefSeqYP_001329976.1. NC_009637.1.

3D structure databases

ProteinModelPortalA6VH99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING426368.MmarC7_0758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR65825; ABR65825; MmarC7_0758.
GeneID5329353.
KEGGmmz:MmarC7_0758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMACIDEALT.
ProtClustDBCLSK926359.

Enzyme and pathway databases

BioCycMMAR426368:GHHL-768-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 nameA6VH99_METM7
AccessionPrimary (citable) accession number: A6VH99
Entry history
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)