(data stored in ACNUC10043 zone)

HOGENOM: CLACE1_2_PE187

ID   CLACE1_2_PE187                       STANDARD;      PRT;   358 AA.
AC   CLACE1_2_PE187; Q97MK4;
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; (CLACE1_2.PE187).
GN   OrderedLocusNames=CA_C0192;
OS   CLOSTRIDIUM ACETOBUTYLICUM ATCC 824.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLACE1_2.PE187.
CC       Clostridium acetobutylicum ATCC 824, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:AEEP_CLOAB
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 epimerization of L-Ala-D-Asp.
CC   -!- CATALYTIC ACTIVITY: L-alanyl-D-glutamate = L-alanyl-L-glutamate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family.
CC   -!- GENE_FAMILY: HOG000185903 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q97MK4; -.
DR   EMBL; AE001437; AAK78174.1; -; Genomic_DNA.
DR   PIR; C96923; C96923.
DR   RefSeq; NP_346834.1; NC_003030.1.
DR   HSSP; P27099; 1NU5.
DR   ProteinModelPortal; Q97MK4; -.
DR   SMR; Q97MK4; 1-356.
DR   GeneID; 1116375; -.
DR   GenomeReviews; AE001437_GR; CA_C0192.
DR   KEGG; cac:CA_C0192; -.
DR   NMPDR; fig|272562.1.peg.363; -.
DR   OMA; LYADANE; -.
DR   PhylomeDB; Q97MK4; -.
DR   ProtClustDB; CLSK882327; -.
DR   BioCyc; CACE272562:CAC0192-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:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
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; 1.
DR   PROSITE; PS00909; MR_MLE_2; FALSE_NEG.
DR   HOGENOMDNA; CLACE1_2.PE187; -.
KW   putative chloromuconate cycloisomerase;
KW   Cell wall biogenesis/degradation; Complete proteome; Isomerase;
KW   Magnesium; Metal-binding; Reference proteome.
SQ   SEQUENCE   358 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIIKDIVIGH LSVPLKKPFK TAVRSVNSVN DVVVKIITDT GNVGFGSAAS TGLVTGDITE
     SIEGAINNYI KRSIVGMDIE DFEAILIKLD NCIVGNTSAK AAVDIALYDL YGQRYGAPLY
     KLLGGFRNKL ETDITISVNS PEEMSRDSVD AVKLGYKTLK IKVGKNPKLD IKRMREIRKA
     IGYEVNLRID ANQGWQPKEA IRALNEIENE GLKIELVEQP VKAWNLEGLK MVTDNVNIPV
     MADESVFSPK DAARVMEMRA CDLINIKLMK TGGIHNALKI CALAEVYGME CMLGCMLEGK
     VSVTAAVHLA AAKRIITKID LDGPVLCSRD DVVGGAMYDN SNIVLVDEPG LGIEGINN
//

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