ID Q1N3Q8_9GAMM Unreviewed; 589 AA.
AC Q1N3Q8;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Acyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:EAT12816.1};
GN ORFNames=RED65_12124 {ECO:0000313|EMBL:EAT12816.1};
OS Bermanella marisrubri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bermanella.
OX NCBI_TaxID=207949 {ECO:0000313|EMBL:EAT12816.1, ECO:0000313|Proteomes:UP000004263};
RN [1] {ECO:0000313|EMBL:EAT12816.1, ECO:0000313|Proteomes:UP000004263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RED65 {ECO:0000313|EMBL:EAT12816.1,
RC ECO:0000313|Proteomes:UP000004263};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (MAR-2006) 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 -!- 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:EAT12816.1}.
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DR EMBL; AAQH01000004; EAT12816.1; -; Genomic_DNA.
DR RefSeq; WP_007018706.1; NZ_CP051183.1.
DR AlphaFoldDB; Q1N3Q8; -.
DR STRING; 207949.RED65_12124; -.
DR HOGENOM; CLU_018204_12_2_6; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000004263; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004263}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 39..159
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 164..267
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 278..447
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 463..584
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 589 AA; 64518 MW; 6157A0F9EB733C82 CRC64;
MASYKAPLND MNFVLFDVLK ADGLSQLPGF EDATEEMIRA VLEEASKFAE NVFQPTNQDG
DIEGCQYDPE THNVTTPKGF KEAYKTFAEG GWSGLSATTE YGGQGLPHLL KIVVDEMACS
TNLSLGMYPG LSHGAIDALT EHAEQELKDK YLPQLISGEW TGTMCLTEPQ CGTDLGLIRT
KAEPQADGSY NISGTKIWIT GGEHDMVDNI VHLVLAKLPG APDSSKGISL FLVPKFLEDG
SRNPAFCGGL EHKMGIKGSA TCVMNFEGAK GWLIGKENEG LKCMFTMMNA ARIMVGVQGL
GLAEKAYQIS LGFAKERLQS RSLTGPKSPD EKADPIIVHP DVRRMLMQQK VFLEGARCMA
YFTGYHLDLA HKHDDESVRE ESDDIVQIMT PIIKAYLTDE GFFSTDQALQ SMGGSGFTQD
WEVEQLLRDG RIARIYEGTN GIQALDLTGR KLTIKGGRLP KTFFKVMNAM IADLDNAEHQ
EKCKTLLKTL QGALMWLGQE AMKDPEQAGA AATPLLKLFS LCAMSVMWAT MAKKANEGLG
SGKYEDAFYQ GKIKAAEHFF RLALSQAEMH KADIEAGKST LMDMAEGEF
//
