ID A0A1I2IEP8_9ACTN Unreviewed; 471 AA.
AC A0A1I2IEP8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:SFF40118.1};
GN ORFNames=SAMN05216251_11385 {ECO:0000313|EMBL:SFF40118.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF40118.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFF40118.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF40118.1,
RC ECO:0000313|Proteomes:UP000199323};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000256|ARBA:ARBA00034772}.
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DR EMBL; FONG01000013; SFF40118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2IEP8; -.
DR STRING; 380248.SAMN05216251_11385; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000199323; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
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; 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-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; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:SFF40118.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199323}.
FT DOMAIN 381..460
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 47455 MW; 4E7EDF69EFADFA50 CRC64;
MFAEPTPGDG GGAADGRDDG LLSPVAAGTA AEAATGDRAV LQALLDAEAA LTRAQARIGA
APAGAGAAVT AAARAGNFDA RSLALRAGAG GNPVIPLVGD LARAVAQHAP EHVEFVHRGA
TSQDIMDTAL MLVAARTLGV ITADLRRAAV TLGALAAFHR ETPMPGRTLT QHAVPTTFGL
KAAGWRALVL DAHDRLVRVR RSLPAQLGGA AGTLAAFVEP AATADPGIAL LGAFADEVGL
AEPEVPWHAL RTPVADLGGA LAFCAGALGK LAADVLLLGR TETGEVGEGG GGGSSAMPHK
RNPVRATLIA SAARQVPALA AVLYGCLAAE DERPAGAWHA EWQPLREALR LTGGAAEATA
ALCPGLVVSP RRMRANLGLT GGLLLTERLA AHLAPLVGRD AAKARLAELS RQVPDPYADL
AAAVAADPLL GPALSAPDLR ALTDPATATG SAAALTDRAL RREPLPDEPR P
//
