PCAB_ACIAD
ID PCAB_ACIAD Reviewed; 451 AA.
AC Q59092; Q6FBL3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=3-carboxy-cis,cis-muconate cycloisomerase;
DE EC=5.5.1.2;
DE AltName: Full=3-carboxymuconate lactonizing enzyme;
DE Short=CMLE;
GN Name=pcaB; OrderedLocusNames=ACIAD1707;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-49.
RX PubMed=8063101; DOI=10.1016/0378-1119(94)90829-x;
RA Kowalchuk G.A., Hartnett G.B., Benson A., Houghton J.E., Ngai K.-L.,
RA Ornston L.N.;
RT "Contrasting patterns of evolutionary divergence within the Acinetobacter
RT calcoaceticus pca operon.";
RL Gene 146:23-30(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Catalyzes an anti cycloisomerization.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate = 3-carboxy-
CC cis,cis-muconate + H(+); Xref=Rhea:RHEA:23656, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57496, ChEBI:CHEBI:57979; EC=5.5.1.2;
CC -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-
CC 4,5-dihydro-2-furylacetate from 3-carboxy-cis,cis-muconate: step 1/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000305}.
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DR EMBL; L05770; AAC37149.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68549.1; -; Genomic_DNA.
DR RefSeq; WP_004926621.1; NC_005966.1.
DR PDB; 1Q5N; X-ray; 2.30 A; A=1-451.
DR PDBsum; 1Q5N; -.
DR AlphaFoldDB; Q59092; -.
DR SMR; Q59092; -.
DR STRING; 62977.ACIAD1707; -.
DR EnsemblBacteria; CAG68549; CAG68549; ACIAD1707.
DR GeneID; 45234094; -.
DR KEGG; aci:ACIAD1707; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_3_3_6; -.
DR OMA; HRATPMI; -.
DR OrthoDB; 347727at2; -.
DR BioCyc; ASP62977:ACIAD_RS07865-MON; -.
DR UniPathway; UPA00157; UER00265.
DR EvolutionaryTrace; Q59092; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProt.
DR GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.275.10; -; 1.
DR InterPro; IPR019468; AdenyloSucc_lyase_C.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR012789; Protocat_PcaB.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR02426; protocat_pcaB; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Isomerase; Reference proteome.
FT CHAIN 1..451
FT /note="3-carboxy-cis,cis-muconate cycloisomerase"
FT /id="PRO_0000161347"
FT CONFLICT 37
FT /note="A -> Q (in Ref. 1; AAC37149)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..56
FT /note="TVIERAA -> NCDRTCQQ (in Ref. 1; AAC37149)"
FT /evidence="ECO:0000305"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 20..40
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1Q5N"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1Q5N"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 107..143
FT /evidence="ECO:0007829|PDB:1Q5N"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1Q5N"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1Q5N"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 163..188
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 232..258
FT /evidence="ECO:0007829|PDB:1Q5N"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 287..308
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 320..348
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:1Q5N"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 382..399
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 419..425
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:1Q5N"
FT HELIX 435..444
FT /evidence="ECO:0007829|PDB:1Q5N"
SQ SEQUENCE 451 AA; 49316 MW; 831FE94AC6574617 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
