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Q81VF6 (Q81VF6_BACAN) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 110. 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 namesRecommended name:
Alanine racemase RuleBase RU004247 HAMAP-Rule MF_01201

EC=5.1.1.1 RuleBase RU004247 HAMAP-Rule MF_01201
Gene names
Name:dal1 EMBL AAP24291.1
Ordered Locus Names:BA_0252 EMBL AAP24291.1, BAS0238 EMBL AAT52574.1, GBAA_0252 EMBL AAT29333.1
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length389 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. SAAS SAAS020622 RuleBase RU004247 HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS020622 HAMAP-Rule MF_01201

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. RuleBase RU004247 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 site411Proton acceptor; specific for D-alanine By similarity HAMAP-Rule MF_01201
Active site2701Proton acceptor; specific for L-alanine By similarity HAMAP-Rule MF_01201
Binding site411Acetate PDB 3HA1
Binding site1311Chloride 2 PDB 3HA1
Binding site1381Chloride 1 PDB 2VD8
Binding site1381Chloride 2 PDB 3HA1 PDB 2VD9
Binding site1381Substrate By similarity HAMAP-Rule MF_01201
Binding site2161Chloride 3; via amide nitrogen PDB 2VD8 PDB 2VD9
Binding site3171Acetate; via amide nitrogen PDB 3HA1
Binding site3171Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue411N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
Q81VF6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5B55B2C4920D6BA5

FASTA38943,662
        10         20         30         40         50         60 
MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSDVEIFAVV KGNAYGHDYV PVAKIALEAG 

        70         80         90        100        110        120 
ATRLAVAFLD EALVLRRAGI TAPILVLGPS PPRDINVAAE NDVALTVFQK EWVDEAIKLW 

       130        140        150        160        170        180 
DGSSTMKYHI NFDSGMGRIG IRERKELKGF LKSLEGAPFL ELEGVYTHFA TADEVETSYF 

       190        200        210        220        230        240 
DKQYNTFLEQ LSWLKEFGVD PKFVHTANSA ATLRFQGITF NAVRIGIAMY GLSPSVEIRP 

       250        260        270        280        290        300 
FLPFKLEPAL SLHTKVAHIK QVIKGDGISY NVTYRTKTEE WIATVAIGYA DGWLRRLQGF 

       310        320        330        340        350        360 
EVLVNGKRVP IVGRVTMDQF MIHLPCEVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE 

       370        380 
IITTISFRVP RIFIRNGKVV EVINYLNDI 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolsto A.B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames EMBL AAP24291.1 and Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne EMBL AAT52574.1.
[3]"Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P)."
Au K., Ren J., Walter T.S., Harlos K., Nettleship J.E., Owens R.J., Stuart D.I., Esnouf R.M.
Acta Crystallogr. F 64:327-333(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH CHLORIDE.
[4]"Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames)."
Counago R.M., Davlieva M., Strych U., Hill R.E., Krause K.L.
BMC Struct. Biol. 9:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ACETATE AND CHLORIDE.
[5]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor and Ames Ancestor EMBL AAT29333.1.
[6]Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., Sutton G.
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Ames EMBL AAP24291.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP24291.1.
AE017334 Genomic DNA. Translation: AAT29333.1.
AE017225 Genomic DNA. Translation: AAT52574.1.
RefSeqNP_842805.1. NC_003997.3.
YP_016858.1. NC_007530.2.
YP_026523.1. NC_005945.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VD8X-ray1.47A/B1-389[»]
2VD9X-ray2.10A/B1-389[»]
3HA1X-ray1.95A/B1-389[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198094.BA_0252.

Protocols and materials databases

DNASU1087014.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP24291; AAP24291; BA_0252.
AAT29333; AAT29333; GBAA_0252.
AAT52574; AAT52574; BAS0238.
GeneID1087014.
2819200.
2848190.
KEGGban:BA_0252.
bar:GBAA_0252.
bat:BAS0238.

Phylogenomic databases

HOGENOMHOG000031444.
KOK01775.
OMARTEEWIA.
OrthoDBEOG6PP9NJ.

Enzyme and pathway databases

BioCycBANT260799:GJAJ-260-MONOMER.
BANT261594:GJ7F-268-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...

Other

EvolutionaryTraceQ81VF6.

Entry information

Entry nameQ81VF6_BACAN
AccessionPrimary (citable) accession number: Q81VF6
Secondary accession number(s): E9R9C7 expand/collapse secondary AC list , E9R9C8, Q6I4F7, Q6KY59
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)