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A1UC18 (A1UC18_MYCSK) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 59. 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 HAMAP-Rule MF_01201

EC=5.1.1.1 HAMAP-Rule MF_01201
Gene names
Ordered Locus Names:Mkms_1163 EMBL ABL90376.1
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP] EMBL ABL90376.1
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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 site421Proton 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 site1401Substrate By similarity HAMAP-Rule MF_01201
Binding site3191Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01201

Amino acid modifications

Modified residue421N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01201

Sequences

Sequence LengthMass (Da)Tools
A1UC18 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 15FE4CBBB7D4C283

FASTA38340,596
        10         20         30         40         50         60 
MQTSETTVTP TAQVVVDLDA ISHNVALLRD RAGSAQVMPV LKADGYGHGA TEVAKVVLDA 

        70         80         90        100        110        120 
GVTELGVATV GEALALRADG ITAPVLAWLH GPGTDFAPAV QADIQLAVSS VRQLGEILDA 

       130        140        150        160        170        180 
VHRTGMTATL TVKADTGLSR NGVSPAEYPA LLQRLAKAQA EDAVRVRGIM SHLACGDEPD 

       190        200        210        220        230        240 
NPTNDRQAQR LTDMRRQAAD AGVTFEVAHL CNSPAAMTRP DLAFDMVRPG IAVYGQTPIP 

       250        260        270        280        290        300 
ALGDMGLRPA MTLRCPVAQT RSIKAGDGVS YGHTWIAQRD TTVALLPIGY ADGVYRSLSG 

       310        320        330        340        350        360 
RLQVLINGRL RPGVGRICMD QFVVDLGPGP VDVSDGDEAI LFGPGTRGEH TAQDWAEIIG 

       370        380 
TINYEIVTSP RGRVVRTYRR ESR 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS EMBL ABL90376.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000518 Genomic DNA. Translation: ABL90376.1.
RefSeqYP_937166.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1UC18.
SMRA1UC18. Positions 12-379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189918.Mkms_1163.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL90376; ABL90376; Mkms_1163.
GeneID4614541.
KEGGmkm:Mkms_1163.
PATRIC18101269. VBIMycSp70743_1681.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031444.
KOK01775.
OMAITMDQLM.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycMSP189918:GH4X-1171-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.
[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.
ProtoNetSearch...

Entry information

Entry nameA1UC18_MYCSK
AccessionPrimary (citable) accession number: A1UC18
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)