(data stored in ACNUC10043 zone)

HOGENOM: BASUB1_1_PE1319

ID   BASUB1_1_PE1319                      STANDARD;      PRT;   366 AA.
AC   BASUB1_1_PE1319; O34508; Q796M5;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=L-Ala-D/L-Glu epimerase; Short=AE epimerase; Short=AEE;
DE   EC=5.1.1 n1; (BASUB1_1.PE1319).
GN   Name=ykfB; OrderedLocusNames=BSU12980;
OS   BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BASUB1_1.PE1319.
CC       Bacillus subtilis subsp. subtilis str. 168 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:AEEP_BACSU
CC   -!- FUNCTION: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-
CC       Glu and has probably a role in the metabolism of the murein
CC       peptide, of which L-Ala-D-Glu is a component. Is also able to
CC       catalyze the reverse reaction and the epimerization of the other
CC       Ala-X dipeptides L-Ala-L-Asp, L-Ala-L-Leu, L-Ala-L-Met, and L-Ala-
CC       L-Ser. Is not able to epimerize other L-Ala-X dipeptides. Is also
CC       active with L-Ser-L-Glu and, oddly, L-Pro-L-Glu, but not with L-
CC       Glu-L-Glu, L-Lys-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala.
CC   -!- CATALYTIC ACTIVITY: L-alanyl-D-glutamate = L-alanyl-L-glutamate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=320 uM for L-Ala-D-Glu (at pH 8.5);
CC         KM=28 uM for L-Ala-D-Asp (at pH 8.5);
CC         KM=510 uM for L-Ala-D-Met (at pH 8.5);
CC         Note=The catalytic efficiency is 25-fold higher with L-Ala-D-Glu
CC         than with L-Ala-D-Asp or L-Ala-D-Met as substrate;
CC   -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers.
CC   -!- INDUCTION: Repressed by AbrB, a transcription factor that
CC       negatively controls biofilm formation.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family.
CC   -!- GENE_FAMILY: HOG000185903 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; O34508; Q796M5; -.
DR   EMBL; AJ002571; CAA05578.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13155.1; -; Genomic_DNA.
DR   PIR; H69855; H69855.
DR   RefSeq; NP_389181.1; NC_000964.3.
DR   PDB; 1JPM; X-ray; 2.25 A; A/B/C/D=1-366.
DR   PDB; 1TKK; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-366.
DR   PDBsum; 1JPM; -.
DR   PDBsum; 1TKK; -.
DR   ProteinModelPortal; O34508; -.
DR   SMR; O34508; 1-359.
DR   EnsemblBacteria; EBBACT00000001248; EBBACP00000001248; EBBACG00000001246.
DR   GeneID; 939862; -.
DR   GenomeReviews; AL009126_GR; BSU12980.
DR   KEGG; bsu:BSU12980; -.
DR   NMPDR; fig|224308.1.peg.1300; -.
DR   GenoList; BSU12980; -.
DR   GeneTree; EBGT00050000001324; -.
DR   OMA; LYADANE; -.
DR   PhylomeDB; O34508; -.
DR   ProtClustDB; CLSK887157; -.
DR   BioCyc; BSUB:BSU12980-MON; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016855; F:racemase and epimerase activity, acting on amino acids and derivatives; IEA:EC.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N.
DR   InterPro; IPR001354; MR_MLE.
DR   PANTHER; PTHR13794; MR_MLE; 1.
DR   Pfam; PF01188; MR_MLE; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   PROSITE; PS00908; MR_MLE_1; FALSE_NEG.
DR   PROSITE; PS00909; MR_MLE_2; FALSE_NEG.
DR   HOGENOMDNA; BASUB1_1.PE1319; -.
KW   3D-structure; Cell wall biogenesis/degradation; Complete proteome;
KW   Isomerase; Magnesium; Metal-binding; Reference proteome.
SQ   SEQUENCE   366 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKIIRIETSR IAVPLTKPFK TALRTVYTAE SVIVRITYDS GAVGWGEAPP TLVITGDSMD
     SIESAIHHVL KPALLGKSLA GYEAILHDIQ HLLTGNMSAK AAVEMALYDG WAQMCGLPLY
     QMLGGYRDTL ETDYTVSVNS PEEMAADAEN YLKQGFQTLK IKVGKDDIAT DIARIQEIRK
     RVGSAVKLRL DANQGWRPKE AVTAIRKMED AGLGIELVEQ PVHKDDLAGL KKVTDATDTP
     IMADESVFTP RQAFEVLQTR SADLINIKLM KAGGISGAEK INAMAEACGV ECMVGSMIET
     KLGITAAAHF AASKRNITRF DFDAPLMLKT DVFNGGITYS GSTISMPGKP GLGIIGAALL
     KGEKEQ
//

If you have problems or comments...

PBIL Back to PBIL home page