ID N9P1Y6_9GAMM Unreviewed; 593 AA.
AC N9P1Y6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Acyl-CoA dehydrogenase C-terminal domain-containing protein {ECO:0000313|EMBL:QQN88579.1};
GN ORFNames=F897_00037 {ECO:0000313|EMBL:ENX11761.1}, IAQ69_02475
GN {ECO:0000313|EMBL:QQN88579.1};
OS Acinetobacter variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70346 {ECO:0000313|EMBL:ENX11761.1, ECO:0000313|Proteomes:UP000013101};
RN [1] {ECO:0000313|EMBL:ENX11761.1, ECO:0000313|Proteomes:UP000013101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2171 {ECO:0000313|EMBL:ENX11761.1,
RC ECO:0000313|Proteomes:UP000013101};
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 Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 2171.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QQN88579.1, ECO:0000313|Proteomes:UP000596079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XM9F202-2 {ECO:0000313|EMBL:QQN88579.1,
RC ECO:0000313|Proteomes:UP000596079};
RA Peng K., Li R.;
RT "Emergence of ISAba1-mediated novel tet(X) in Acinetobacter variabilis from
RT a chicken farm.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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; APRS01000001; ENX11761.1; -; Genomic_DNA.
DR EMBL; CP060811; QQN88579.1; -; Genomic_DNA.
DR RefSeq; WP_005232064.1; NZ_KB850111.1.
DR AlphaFoldDB; N9P1Y6; -.
DR STRING; 70346.F897_00037; -.
DR PATRIC; fig|1217693.3.peg.31; -.
DR HOGENOM; CLU_018204_12_2_6; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000013101; Unassembled WGS sequence.
DR Proteomes; UP000596079; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 4..27
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 36..158
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 163..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 468..584
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 593 AA; 64798 MW; A60F5B144720B35F CRC64;
MPIYNAPLAD MKFILNDVFN AEQFWQANEN LAHLDTATAE AILEEMAKFA QNVMLPLNRT
GDEEGAKYEN GNVTTPAGFK EAFKQYAEGG WIGLGADAEW GGQEMPKMLT VLSDEMLFAT
NPSFMLYPLL SVGAGMALNS YASQEQKETY LPKIYSGEWS GTMCLTEPHA GTDLGIIKTK
AERNEDGTYS ITGTKIFITG GDHDLAENII HLVLAKTPDA PAGSRGISLF IVPKFLVNED
GSIGERNPVG PGSIEHKMGI KASATCVMNF DGAKGYLVGK ENEGLAAMFV MMNYERLSMG
IQGLGASEFA YQNAAQYATD RLQGRSALGA QSPAKPADSI LVHGDVRRML LNVRANNEAS
RAFAVYVGQQ LDITKFSTDP EAVKKANDRV ALLTPIAKAY LTDTAFQATL DAQMVFGGHG
YIREWGMEQC IRDLRISQIY EGTNGVQSQD LIGRKTIKCG GAYIGEYIEE IRDFANQLDA
DLNFIKDATL DAATEVESLT QFVLEAAGEN AEFPNAAAVD YLHAVGLLSF SYMFARIANA
AKDKDGEFYQ NKLALARYFT QRILPELALR ITKVKAGCEV VMNFSEDYFT TQA
//
