ID I4F4C2_9ACTN Unreviewed; 443 AA.
AC I4F4C2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:CCH90485.1};
DE EC=5.5.1.2 {ECO:0000313|EMBL:CCH90485.1};
GN Name=pcaB {ECO:0000313|EMBL:CCH90485.1};
GN OrderedLocusNames=MODMU_5106 {ECO:0000313|EMBL:CCH90485.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH90485.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH90485.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH90485.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000256|ARBA:ARBA00034772}.
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DR EMBL; FO203431; CCH90485.1; -; Genomic_DNA.
DR RefSeq; WP_014743040.1; NC_017955.1.
DR AlphaFoldDB; I4F4C2; -.
DR STRING; 477641.MODMU_5106; -.
DR KEGG; mmar:MODMU_5106; -.
DR PATRIC; fig|477641.3.peg.4799; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_3_2_11; -.
DR OMA; MDVKLMM; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
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 PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:CCH90485.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 30..295
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
SQ SEQUENCE 443 AA; 44191 MW; 8E22BB3614FBEEB1 CRC64;
MSILDATFAR GPVSAGGPAA DPWLVALLEV EGALARAAAR VGLVAGTAAD EVSRVCADPG
GLDLAAVQVR AADAGNPVPP LVRALQDAVG PHAARAVHVG ATSQDVMDTA AVLLARRGLQ
LIEADLATAA EACARLATEH RDDVLMGRTL LQQALPITVG LKAATWLAGL DGVRARLTAV
SGSLPVQYGG AVGTLAASSG SGVDLRRELA AELGLAVTDV PWFTVRLPVA DVAGVLGAAA
GVVATIAVDV VLLAQSEVAE ATEVSASRGG SSAMPHKNNP VAAVSARACA RRAPGLVATL
YAAMEQEHER GAGTWHVEWP TLTELLGTVG SAASWLTECL ADLQLDTTRM AAAVAAAGDP
QLARALAEAL TPSLGAGAAH DAASAAVRTA ASEGRALVDV VLERADVDGA ALVADSTPDV
GEAGAQVDAA LAAHVIATQG GRP
//
