ID A0A0F0KBU9_9MICO Unreviewed; 414 AA.
AC A0A0F0KBU9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dibenzothiophene desulfurization enzyme C {ECO:0000313|EMBL:KJL17879.1};
GN Name=soxC {ECO:0000313|EMBL:KJL17879.1};
GN ORFNames=RN50_02983 {ECO:0000313|EMBL:KJL17879.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL17879.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL17879.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL17879.1,
RC ECO:0000313|Proteomes:UP000033572};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL17879.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYIU01000046; KJL17879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0KBU9; -.
DR PATRIC; fig|104336.4.peg.3021; -.
DR Proteomes; UP000033572; Unassembled WGS sequence.
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:UP000033572}.
FT DOMAIN 38..120
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 250..388
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 414 AA; 45311 MW; BD49F9B40FEDDCBD CRC64;
MTITDAVTTG LGDRWREGAR PQTTDEWLAR AQEVADILAV DAVERDRANQ TPHAEVQLLK
DSGLVTLLGP RAHGGAGETW DTAYRVIRTV ARGDGSIGQV LGYHYLWAWA ARLVGTEEQI
AAVEELYTSN ALVFGGAVNP RDSDLVIRED GDDLVFSGRK SFSTGGQISD LTVLEGVLEG
SDTHIFAIVP TAQDGIVFAD DWDSLGQRLT ESGSVEIRDV RVPWAAAAGF VDRVFRPLTY
NTLNVPTIQL VFANFYLGIA QGALETASAY TRTRTRPWPY GGDDKQHATD EWYLLEGYGE
LASTLWADEA LLDAVGGEIS AVLHAPREEL TPRRRGEIAV RVAAGKLRVV DDGLTVATKV
YELTGARASA SSVGLDIFWR NLRTHSLHDP IAYKKREVGT FVLKNEVPEP TWYT
//
