ID F2JTL0_MARM1 Unreviewed; 582 AA.
AC F2JTL0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:ADZ91524.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:ADZ91524.1};
GN OrderedLocusNames=Marme_2283 {ECO:0000313|EMBL:ADZ91524.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91524.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ91524.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
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}.
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DR EMBL; CP002583; ADZ91524.1; -; Genomic_DNA.
DR RefSeq; WP_013661429.1; NZ_CP047696.1.
DR AlphaFoldDB; F2JTL0; -.
DR STRING; 717774.Marme_2283; -.
DR KEGG; mme:Marme_2283; -.
DR PATRIC; fig|717774.3.peg.2353; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_6; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000001062; Chromosome.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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 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:UP000001062}.
FT DOMAIN 70..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..267
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 462..574
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 582 AA; 63310 MW; F251A24D85C55E83 CRC64;
MSDYRYPYKD VLFALNHVAN IGRLNDLVDE PLSQDLLEAI LTESAKLSEQ IIAPLNWSGD
QQGAELREGE VYEAEGFKEA FRSYVEGGWA SLSGDEVYGG QGLPSTLATA VNEGIQSANL
AFSLCPLLSN GAIEALEKYG SQLLKDTYLE KLVSGEWTGT MNLTEPNAGS DLAAIRTKAT
PHEDHFLIQG QKIFITWGDH QMSENIVHLV LARLPDAPEG VKGISLFVVP KFLVDENGAL
GRRNDVSVAS LEHKMGIHAS PTCVMAFGET SGAVGYLVGE PNQGLKAMFA MMNNARQGVG
LQGLAIAERA YQQALEYAQE RVQGYDSSRK NRVAIVAHPD VKRMLMTMKS LIDASRLLIY
VAAVENDVSK LAVGDQAKTA AELTALYTPV VKGWITEIAQ EVTSLAVQVH GGMGFIEETG
VAQHARDARI LPIYEGTNGI QAIDLIGRKL LGDNASAMAT LINQIVADVH ASQSKYSEAV
LSEVALFKQT TTVCLESMKE NSTLGTYNAY PYMMQFGYVL GAWLMLKAQA ETALEGESAS
NEERLRCASI DFYCQQILPR ARLFGSMIEN GTEDVDVSIF KQ
//
