ID K2GRH5_9BACI Unreviewed; 593 AA.
AC K2GRH5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EKE33004.1};
GN ORFNames=MJ3_00850 {ECO:0000313|EMBL:EKE33004.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE33004.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE33004.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE33004.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(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}.
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:EKE33004.1}.
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DR EMBL; AMPQ01000001; EKE33004.1; -; Genomic_DNA.
DR RefSeq; WP_008587188.1; NZ_JAFBFF010000001.1.
DR AlphaFoldDB; K2GRH5; -.
DR STRING; 1230341.AAV35_003635; -.
DR KEGG; sje:AAV35_003635; -.
DR PATRIC; fig|1230341.3.peg.183; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000011746; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
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; 2.
DR InterPro; IPR049426; Acyl-CoA-dh-like_C.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF21263; Acyl-CoA-dh_C; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000011746}.
FT DOMAIN 30..142
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 146..238
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..414
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 462..565
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 593 AA; 65494 MW; 76F651305F1E57C6 CRC64;
MSDVKDMIKG GSFLVEDVEA EDIITPEDFT EEHKMIAKTT EDFITGDVLP KVDKIENHEF
EHSLELMKKA GELGLLGADV PEEYGGVQLD KISSSLITEK FARAGGFSLT HGAHVGIGSL
PIVFFGNSDQ KKKYLPKLAT GELLAAYALT EPGSGSDARG AKTTAKLNEA GTHYVLNGEK
QWITNSAFAD VFIVYAKIDG EKFTAFIVER EHPGVSTGPE EKKMGIKGSS TRTLILEDAE
VPVENVLGEI GRGHIIAFNI LNVGRYKLAI GSVGSAKRAI ELSVNYAQER KQFDTPIMSF
PLIKEKVASV AANTYANESA VYRTVGLFEQ SMGRLSEEEL NDGKAVANVI AEYAIECSLT
KVFGSELLDF AVDEAVQIHG GYGFMQEYEV ERMYRDSRIN RIFEGTNEIN RMIVPGNLVK
KAMKGELPIF EKAKKLQEEI MTMMPEEPGD APLEQEFYLL KNAKKIALLA SGLAAQKYGE
KLDQEQEVLV NLADITGEIF NMESAILRTK KAVDKDGAEK HSQKLLYTEV YVQEAFNRIE
AHAKETLIAA EEGDDLRMML GALRKLTRHN PVNVIKKKRE ISVGLEKAGK YFV
//
