ID A0A0N1FNZ7_9ACTN Unreviewed; 448 AA.
AC A0A0N1FNZ7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:KPH98994.1};
DE EC=5.5.1.2 {ECO:0000313|EMBL:KPH98994.1};
GN ORFNames=OK074_6119 {ECO:0000313|EMBL:KPH98994.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPH98994.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPH98994.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPH98994.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPH98994.1}.
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DR EMBL; LJCV01000300; KPH98994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1FNZ7; -.
DR PATRIC; fig|1592327.3.peg.8999; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
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; 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:KPH98994.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 370..445
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
FT REGION 424..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 46187 MW; 7792CAAC8C934992 CRC64;
MTSPPPVRPT ADAGLLAPGW TGSPAAEATG DTAYLRALLD AEAALTRAQA AAGLAPAGAA
TAVTAAADPA RFDVRSLAER ARGGGNPVIP LVADLTKAVG AEYGPYVHRG ATSQDILDTA
TMLVAARTLG LVLDDLARTA RALARLAAEH RDSAMPGRTL TQHAVPTTFG LKAAGWRALV
LDARDRLTAV RDGLPAQLGG AAGTLAAFTA YGAGDATGLV AAYARELGLR APELPWHTLR
TPVADLAGAL AFTAGALGKL AVDVLTLART EIAEVAEGSG GGSSAMPHKA NPVRSTLIAA
ASARAPQLAA TLYGSLAAGD ERPAGAWHAE WEPLRDLLRL VGGAARDAAE LTEGLRVYAD
VMRQHLDLTH GLIVSERLSA ELASVLGRTR AKELLTQLAA RTYAEGRPLR ELLAEEPELK
DVDLDDLTDP ARYTGSAGAL TDRALERP
//
