(data stored in ACNUC15324 zone)

HOGENOM: ACIAD_1_PE1562

ID   ACIAD_1_PE1562                       STANDARD;      PRT;   451 AA.
AC   ACIAD_1_PE1562; Q59092; Q6FBL3;
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=3-carboxy-cis,cis-muconate cycloisomerase; EC=5.5.1
DE   2;AltName: Full=3-carboxymuconate lactonizing enzyme; Short=CMLE;
DE   (ACIAD_1.PE1562).
GN   Name=pcaB; OrderedLocusNames=ACIAD1707;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE1562.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PCAB_ACIAD
CC   -!- FUNCTION: Catalyzes an anti cycloisomerization.
CC   -!- CATALYTIC ACTIVITY: 2-carboxy-2,5-dihydro-5-oxofuran-2-acetate =
CC       cis,cis-butadiene-1,2,4-tricarboxylate.
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       5-oxo-4,5-dihydro-2-furylacetate from 3-carboxy-cis,cis-muconate:
CC       step 1/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC   -!- GENE_FAMILY: HOG000033914 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q59092; Q6FBL3; -.
DR   EMBL; L05770; AAC37149.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68549.1; -; Genomic_DNA.
DR   RefSeq; YP_046371.1; NC_005966.1.
DR   PDB; 1Q5N; X-ray; 2.30 A; A=1-451.
DR   PDBsum; 1Q5N; -.
DR   ProteinModelPortal; Q59092; -.
DR   SMR; Q59092; 3-446.
DR   STRING; Q59092; -.
DR   GeneID; 2879432; -.
DR   GenomeReviews; CR543861_GR; ACIAD1707.
DR   KEGG; aci:ACIAD1707; -.
DR   NMPDR; fig|62977.3.peg.1633; -.
DR   eggNOG; COG0015; -.
DR   OMA; HRATPMI; -.
DR   ProtClustDB; CLSK707358; -.
DR   BioCyc; ASP62977:ACIAD1707-MON; -.
DR   GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019619; P:protocatechuate catabolic process; IEA:InterPro.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C_met/fun.
DR   InterPro; IPR003031; D_crystallin.
DR   InterPro; IPR000362; Fumarate_lyase.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR024083; L-Aspartase-like_N.
DR   InterPro; IPR022761; Lyase1_N.
DR   InterPro; IPR012789; Protocat_PcaB.
DR   Gene3D; G3DSA:1.10.275.10; G3DSA:1.10.275.10; 1.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-Aspartase-like; 1.
DR   TIGRFAMs; TIGR02426; Protocat_pcaB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
DR   HOGENOMDNA; ACIAD_1.PE1562; -.
KW   3D-structure; Aromatic hydrocarbons catabolism; Complete proteome;
KW   Direct protein sequencing; Isomerase.
SQ   SEQUENCE   451 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQLYASLFY QRDVTEIFSD RALVSYMVEA EVALAQAQAQ VGVIPQSAAT VIERAAKTAI
     DKIDFDALAT ATGLAGNIAI PFVKQLTAIV KDADEDAARY VHWGATSQDI LDTACILQCR
     DALAIVQNQV QQCYETALSQ AQTYRHQVMM GRTWLQQALP ITLGHKLARW ASAFKRDLDR
     INAIKARVLV AQLGGAVGSL ASLQDQGSIV VEAYAKQLKL GQTACTWHGE RDRIVEIASV
     LGIITGNVGK MARDWSLMMQ TEIAEVFEPT AKGRGGSSTM PHKRNPVAAA SVLAAANRVP
     ALMSSIYQSM VQEHERSLGA WHAEWLSLPE IFQLTAGALE RTLDVLKGME VNAENMHQNI
     ECTHGLIMAE AVMMALAPHM GRLNAHHVVE AACKTAVAEQ KHLKDIISQV DEVKQYFNPS
     QLDEIFKPES YLGNIQDQID AVLQEAKGEA K
//

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