ID   A0A0C2LW32_9CYAN        Unreviewed;       627 AA.
AC   A0A0C2LW32;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Cyclase {ECO:0000313|EMBL:KIJ79091.1};
GN   ORFNames=SD81_07560 {ECO:0000313|EMBL:KIJ79091.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ79091.1};
RN   [1] {ECO:0000313|EMBL:KIJ79091.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ79091.1};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIJ79091.1}.
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DR   EMBL; JXCB01000004; KIJ79091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2LW32; -.
DR   OrthoDB; 5365325at2; -.
DR   GO; GO:0004061; F:arylformamidase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   Gene3D; 3.50.30.50; Putative cyclase; 1.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR007325; KFase/CYL.
DR   InterPro; IPR037175; KFase_sf.
DR   PANTHER; PTHR31118; CYCLASE-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR31118:SF12; CYCLASE-LIKE PROTEIN 2; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF04199; Cyclase; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF102198; Putative cyclase; 1.
PE   4: Predicted;
FT   DOMAIN          2..112
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   REGION          367..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  68641 MW;  D189E4926EBC0F94 CRC64;
     MKDHHSLLDT AKSYLLEEVA PLANEIDCNP TALFQALRGF GELGMLALLV PRQWGGQKVS
     EQIYGSFQEL VARYSGALAF LQTQHQSAAG MLVASSNSLL QEKYLPRMSN GEVLLGVGFS
     QLRREGDPLT VATPVGGGYQ LNGVVPWVTG QGFFSEFIVA ATLPDGGAVF GVVPLRETHQ
     ESGGAMTLST SAQLAAMTST NTVTASLKNW FLPTESVVFM KPAGWIHEND KKNVLRATFL
     ATGCAFAGLD ILESVARTKS LPFITNAFDS LQQELRNCRT AVEEAQNNSG LELAERLQLR
     AWAIDLAGRI AHAAVTVSSG AALYSSHDAQ RVYREALVFT VTGQTRAVME ATLLRLTRRS
     FYNQPQRRRG GHFRAGVPPV EESVRQRREE REENRQISYS RVIHLSHVID TDIPQWQGDP
     PVEFETVAQL HKDGYYLRRF FMGEHSATHI NAPNSFHLDG VGIDEYSAES LVVPAVVIDI
     GEKVLGNSDY ALTVGDILAW EKHYGGIPSG SVVLVYTGWQ EKWLDKNAFF NQDAQGRMHF
     PGFSRDATRF LVEERQIAGV GIDTHGVDSG QDTTFATNRL VLERQGIVLE NLTNLDQLPS
     TGATLVIGVL RLRAGSGSPV GVLAFLP
//