ID D9PI42_9ZZZZ Unreviewed; 573 AA.
AC D9PI42;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EFK96782.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:EFK96782.1};
GN ORFNames=LDC_1196 {ECO:0000313|EMBL:EFK96782.1};
OS sediment metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=749907 {ECO:0000313|EMBL:EFK96782.1};
RN [1] {ECO:0000313|EMBL:EFK96782.1}
RP NUCLEOTIDE SEQUENCE.
RG CONSOLIDER consortium CSD2007-00005;
RA Guazzaroni M.-E., Richter M., Garcia-Salamanca A., Yarza P., Ferrer M.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFK96782.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21735153; DOI=10.1007/s00248-011-9903-y;
RA Ferrer M., Guazzaroni M.E., Richter M., Garcia-Salamanca A., Yarza P.,
RA Suarez-Suarez A., Solano J., Alcaide M., van Dillewijn P.,
RA Molina-Henares M.A., Lopez-Cortes N., Al-Ramahi Y., Guerrero C., Acosta A.,
RA de Eugenio L.I., Martinez V., Marques S., Rojo F., Santero E.,
RA Genilloud O., Perez-Perez J., Rossello-Mora R., Ramos J.L.;
RT "Taxonomic and Functional Metagenomic Profiling of the Microbial Community
RT in the Anoxic Sediment of a Sub-saline Shallow Lake (Laguna de Carrizo,
RT Central Spain).";
RL Microb. Ecol. 62:824-837(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:EFK96782.1}.
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DR EMBL; ADZX01000404; EFK96782.1; -; Genomic_DNA.
DR AlphaFoldDB; D9PI42; -.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 1.
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; IPR020964; Acyl-CoA_dehydrogenase_C.
DR InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12186; AcylCoA_dehyd_C; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF158494; PG0775 C-terminal 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EFK96782.1}.
FT DOMAIN 53..169
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 173..267
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..364
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 390..446
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 458..559
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12186"
SQ SEQUENCE 573 AA; 65030 MW; FD36A03E7C6BE172 CRC64;
MANFFTDNQD LLFQFERLNL KEVVDFYEEN YKQSEKYNYA PINYEDAKEN YRRILEITGD
IAANYIAPRS PSIDDEGAVF KDGKVQYAKG TKESLDLLSK AELMGMILPR AYGGLNFPTT
IYMVAVEMIS RADASLMNIF GLQDIGRTIA EFGNNEQKQE FLPSFSSGKY TAAMALTEPD
AGSDLQAVKL TAYQDEKGNW FLRGVKRFIT NGNGEVLLVL ARTEAGTKDA RGLSMLVCYG
DETVKVRRIE HKLGIHGSPT CELQFNDTPA QLVGSRRFGL LKYVMYLMNR ARVGIGAQSL
GIAQEAYEQA LKYAKAREQF GKPIYNFPVV SNMLIDMRVS LEAFRSLFYN TCVWLDKKEM
LEQMVDKLKL EKKPVAETNE RLKEATKYLN LLTPLAKYFL SEGVNKICYD SMQIHGGTGY
MHEFGIERLS RDARITNIYE GTSQLQVVAA SGGVINDVFA DHFTDCEKKE YKGSLINLLS
VLKEIRELFA DCLKYIKEKK DPNIQDVAAK DLVELYGYIY VGFLLLDEAN EDQRKVFTAR
RYILDALTKA RKNAEAIKNE LYSDILYADT ILI
//
