ID A0A178GPM9_9GAMM Unreviewed; 393 AA.
AC A0A178GPM9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:OAL87400.1};
GN ORFNames=AY605_03370 {ECO:0000313|EMBL:OAL87400.1};
OS Acinetobacter sp. SFD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1805635 {ECO:0000313|EMBL:OAL87400.1, ECO:0000313|Proteomes:UP000186186};
RN [1] {ECO:0000313|EMBL:OAL87400.1, ECO:0000313|Proteomes:UP000186186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFD {ECO:0000313|EMBL:OAL87400.1,
RC ECO:0000313|Proteomes:UP000186186};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:OAL87400.1}.
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DR EMBL; LSZJ01000001; OAL87400.1; -; Genomic_DNA.
DR RefSeq; WP_064095043.1; NZ_LSZJ01000001.1.
DR AlphaFoldDB; A0A178GPM9; -.
DR STRING; 1805635.AY605_03370; -.
DR Proteomes; UP000186186; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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 Monooxygenase {ECO:0000313|EMBL:OAL87400.1};
KW Oxidoreductase {ECO:0000313|EMBL:OAL87400.1}.
FT DOMAIN 19..113
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 234..368
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 393 AA; 43776 MW; 4D0E38D3EDBF7743 CRC64;
MNAQSPYLNQ SPVDIAQKLA ENFALTAAER DKQGGNPKAE RDLIRQSGLL GLSIPKQYGG
QEADWQTIFK TIQIMAQVDS SLAHVYGFHH LLIATVQLFS QAEQYGPWFE QTAQNNLFWG
NTLNPLDRRT TATKVSENEY IFHGDKSFCS GSIDSDMLLC SGYNDAGKLL IGVIPTQRKG
VSFLGDWNNM GQRQTDSGTS HFEQVKIHQN ELLLNPGPLS TPYSSLRPLI AQLIFVHLFL
GVAEGAFDVA KQTVQTQKAW SKSLVEDAVN DPFIQKHFAE FYVQLEGVRL LADKAVQALQ
AAWELGNDLS AEQRGEVSVA IATAKIAATN TSLYITQNIF QVMGARATTA KLNLDRFWRN
VRTQTLHDPI DYKYQEVGEW VLTGKVPDPS FYS
//
