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Database: UniProt
Entry: K9RIC6_9CYAN
LinkDB: K9RIC6_9CYAN
Original site: K9RIC6_9CYAN 
ID   K9RIC6_9CYAN            Unreviewed;       614 AA.
AC   K9RIC6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Putative metal-dependent hydrolase {ECO:0000313|EMBL:AFY57059.1};
GN   ORFNames=Riv7116_4640 {ECO:0000313|EMBL:AFY57059.1};
OS   Rivularia sp. PCC 7116.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae;
OC   Rivularia.
OX   NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY57059.1, ECO:0000313|Proteomes:UP000010380};
RN   [1] {ECO:0000313|EMBL:AFY57059.1, ECO:0000313|Proteomes:UP000010380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY57059.1,
RC   ECO:0000313|Proteomes:UP000010380};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003549; AFY57059.1; -; Genomic_DNA.
DR   RefSeq; WP_015120619.1; NC_019678.1.
DR   AlphaFoldDB; K9RIC6; -.
DR   STRING; 373994.Riv7116_4640; -.
DR   KEGG; riv:Riv7116_4640; -.
DR   PATRIC; fig|373994.3.peg.4952; -.
DR   eggNOG; COG1878; Bacteria.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_463646_0_0_3; -.
DR   OrthoDB; 5365325at2; -.
DR   Proteomes; UP000010380; Chromosome.
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; 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;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:AFY57059.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010380}.
FT   DOMAIN          17..120
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   COILED          353..380
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   614 AA;  66985 MW;  C7E542366214911C CRC64;
     MDSSAKVSLQ NIPSFFNAAK SYLSETIALR ANEIDESPRA LCEALRGLGD LNLLALKVLQ
     KWGGKEVSGL DYGSFQQLVA RYSGALAFLQ TQHQSAAGIL AAGNNPQLQQ KYLPHMGSGE
     ILLGVGFSHL RRRGEPIITA YKVASGYRIN GVVPWITGFG LFQEFVIAAT LDNGGAVFGI
     APFQNIQQAQ KGEITFTSPA QMAAMNSTNT VSATLDNWFL PEEFVISIKP PGWIQENDKK
     NLLNATFLAF GCAEAGLDVI QAEFNKKSLF FIEDAFISLQ AELKRCRSAI IEAQQQQVEF
     ERKLQLRAWA IDLTSRIAHA AVTASSGAAN YSLSAAQRVY REALVFTVTG QSSAIMEATL
     ARLTRNAPDL EQEETILQDK NPNLISYSRV VHLSHVIDTN IPRWEGDPIV EFETVADLQE
     QGYYLRRFSM GEHSATHINA PVSFHGDGIA IDRYPADSLV LSAVLIDISS SVAINPDYAL
     TIDDIDAWEN QHGKIAGKSV VLLKTGWQEK WHDEKAFFNK DAGGLMHFPG FNVDATQFLV
     NNRNIAGIGI DTHGVDGGSD VNFSINRLVL DKPRIVLENL TNLEQLPAKG ITIIIGALRL
     RGGSGSPASV LALI
//
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