ID S3MVN0_9GAMM Unreviewed; 388 AA.
AC S3MVN0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=F945_02594 {ECO:0000313|EMBL:EPF71562.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF71562.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF71562.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF71562.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) 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:EPF71562.1}.
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DR EMBL; ATGI01000032; EPF71562.1; -; Genomic_DNA.
DR RefSeq; WP_016656991.1; NZ_KE340353.1.
DR AlphaFoldDB; S3MVN0; -.
DR STRING; 632955.GCA_000829675_01354; -.
DR PATRIC; fig|421052.3.peg.2536; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_2_1_6; -.
DR OrthoDB; 7316074at2; -.
DR Proteomes; UP000014568; 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:UP000014568}.
FT DOMAIN 32..93
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 239..366
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 388 AA; 42375 MW; 156FDE5C83758F5A CRC64;
MNNLSTKDFV MSANTTELAA LCQEIRERAC TGEFDQQAYV SQDIINKLKE IGVYRAFVPK
RFGGNEWSPK QFCELIEQLS KADGSVGWVA SFGMSPAYLG SLPEATLEQL YKDSPDLVFA
GGIFPPQPAE ITDDGVVVSG RWKFSSGCMG ADIIGVGISP QKDNEAQGLP RMAVMPAHQA
QIEMTWDTVG LKGTGSHDLV VKDVLVAKEW TFVRGEASKL PEPFFKYPSL SLATQVLTVV
GIGVAAAALE EFQKLAPGKA SITGGAEIAN RPVTQYEFAQ AEAEFRAARV WFYETMQIVW
DEIVQGRKAT AEQISDMRLS CTHAARVCAR VTRKMQMLAG MTAIYTNNPF SRFVNDTHVV
TQHAFMGDAT LQNAGLVSFG MKPTPGYL
//
