ID A0A438MA25_9ACTN Unreviewed; 457 AA.
AC A0A438MA25;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:RVX42573.1};
GN ORFNames=EDD27_5209 {ECO:0000313|EMBL:RVX42573.1};
OS Nonomuraea polychroma.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX42573.1, ECO:0000313|Proteomes:UP000284824};
RN [1] {ECO:0000313|EMBL:RVX42573.1, ECO:0000313|Proteomes:UP000284824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX42573.1,
RC ECO:0000313|Proteomes:UP000284824};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC {ECO:0000256|ARBA:ARBA00034772}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RVX42573.1}.
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DR EMBL; SAUN01000001; RVX42573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438MA25; -.
DR Proteomes; UP000284824; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 2.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
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 PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00206; Lyase_1; 2.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 2.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:RVX42573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284824}.
FT DOMAIN 34..202
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 285..375
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT REGION 199..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 45656 MW; C7423B72265813BC CRC64;
MTSGDVPGAD LGLLSPMRGA AEETGDVAFL RAMLDAEVAL SRAQAALGLV PREAAEAVAA
AARVSAFDLP GLVERARSGG NPVIPLVEDL REAASPFGAY VHLGATSQDI VDTAIMLVAH
RTLGPVLADV DRIVAALTRL AAEHRDTPMA ARTLTQQAVP TTFGLKAAGW RKLAIDARAR
LRAARVSLPA QLGGAAGTLA AFHPTSSPTT PTPGGTHSGP APGALAAGSG GSAVTSSAVG
ASTDTTANGS AEASSPTSGG AAGGGAAGGG AAASGPTAGG AAGDDVGLRL VERFAVEAGL
AEPRLPWHVL RTPVADLAGA LAFTAGALGK MAADVLVLSR TEIGEVSEGV GGGSSSMPHK
HNPVRATMIA TTARQLPALA AILYGGLAAE DERPSGAWHA EWQPLREALR LVAGAARDAA
ELVADLRVHP ERMRANLTLS GSTGSARALV DRALEEE
//
