ID K9TUS5_CHRTP Unreviewed; 408 AA.
AC K9TUS5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AFY86602.1};
GN ORFNames=Chro_1071 {ECO:0000313|EMBL:AFY86602.1};
OS Chroococcidiopsis thermalis (strain PCC 7203).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Chroococcidiopsidaceae; Chroococcidiopsis.
OX NCBI_TaxID=251229 {ECO:0000313|EMBL:AFY86602.1, ECO:0000313|Proteomes:UP000010384};
RN [1] {ECO:0000313|EMBL:AFY86602.1, ECO:0000313|Proteomes:UP000010384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7203 {ECO:0000313|EMBL:AFY86602.1,
RC ECO:0000313|Proteomes:UP000010384};
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., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Chroococcidiopsis thermalis PCC 7203.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003597; AFY86602.1; -; Genomic_DNA.
DR RefSeq; WP_015153151.1; NC_019695.1.
DR AlphaFoldDB; K9TUS5; -.
DR STRING; 251229.Chro_1071; -.
DR KEGG; cthe:Chro_1071; -.
DR PATRIC; fig|251229.3.peg.1272; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_1_3; -.
DR InParanoid; K9TUS5; -.
DR OrthoDB; 571684at2; -.
DR Proteomes; UP000010384; Chromosome.
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 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 InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
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 PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000010384}.
FT DOMAIN 33..126
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 251..372
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 408 AA; 44251 MW; 0C81E4847BE72111 CRC64;
MRKVDTIAPL STNEIGQQKL SLVEVLVKAE EIADFCASNA AAIDVNGAFP VKEFESIAQA
GLLAAPLPPE LGGLGLGIDS SRTWETLQLL KQIGRGNLAV GRIYEGHVNA LQLIQTFGTK
AQIEAYASDA RDRHKIFGVW NAEASDGVKI FPMEDGKFQL QGSKTFASGS GYVERPFASG
ALPDGSWQMC IVPMEEVPTV SDPAWWQPSG MRATASFKVD FSGVELDAGA LIGKPGDYYR
QPWLTTGVIR FAAVQLGGAE SLFNETRKYL DKLGRTLDPY QQTRVGQMAI AIESGNLWLR
GAADLVKAYA PTFAGDANTS NEQADKLVAY ANMVRTAIEQ TCMDVIQLCE RCVGTRGLLP
PIPMERIIRD LTLYLRQPAF DAAIANVGQY ALSESSSAHS LWSYESDN
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