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Database: UniProt
Entry: W5WBS2_9PSEU
LinkDB: W5WBS2_9PSEU
Original site: W5WBS2_9PSEU 
ID   W5WBS2_9PSEU            Unreviewed;       448 AA.
AC   W5WBS2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:AHH95629.1};
DE            EC=5.5.1.2 {ECO:0000313|EMBL:AHH95629.1};
GN   ORFNames=KALB_2260 {ECO:0000313|EMBL:AHH95629.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH95629.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH95629.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH95629.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       {ECO:0000256|ARBA:ARBA00034772}.
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DR   EMBL; CP007155; AHH95629.1; -; Genomic_DNA.
DR   RefSeq; WP_025355802.1; NZ_CP007155.1.
DR   AlphaFoldDB; W5WBS2; -.
DR   STRING; 1449976.KALB_2260; -.
DR   KEGG; kal:KALB_2260; -.
DR   PATRIC; fig|1449976.3.peg.2256; -.
DR   eggNOG; COG0015; Bacteria.
DR   HOGENOM; CLU_030949_3_3_11; -.
DR   Proteomes; UP000019225; Chromosome.
DR   GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   CDD; cd01597; pCLME; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR012789; Protocat_PcaB-like.
DR   NCBIfam; TIGR02426; protocat_pcaB; 1.
DR   PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:AHH95629.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019225}.
FT   DOMAIN          367..441
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   448 AA;  46574 MW;  533D434229FC3581 CRC64;
     MAGTDSGLLA PTWAGTPVAR AVEDEAWLRA MVDVEGALAR AQARLGVIPA AAAEAISAVD
     AGRIDLVELA ERSRAAANPV VAFVPALTAL LPEEAREYVH RGSTSQDILD SATMLVVKRA
     LGLLVPDLRR VAAALAGLAE RHRDTVMAGR TLGQHAVPIT FGLKVATWLQ LVLDALDRIK
     ALVLPAELGG AAGTLAAYVE YAKLSGVDGG VELIEPFAEE LGLAVPVLPW HTARTPLVDV
     AGALQIVTGA LGKIALDVQV LSRTEIGELA EPAAEGRGAS SAMPQKRNPV LATLIVSAAR
     QLPALVSVLA QAMVAEDERP AGAWHAEWQP LREALRLAGG AAHTAAELVE GLEVFPERMA
     STVDVLGGAI VSERLNVALA PVLGKAAAKK VLGAATAEAA RSGRPLREVL AEQVEVDLPL
     DDLLDPARYL GAAGALVDRV LARYRLST
//
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