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Database: UniProt
Entry: A0A2H3L0N8_9CHLR
LinkDB: A0A2H3L0N8_9CHLR
Original site: A0A2H3L0N8_9CHLR 
ID   A0A2H3L0N8_9CHLR        Unreviewed;       545 AA.
AC   A0A2H3L0N8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PDV99875.1};
GN   ORFNames=A9Q02_01295 {ECO:0000313|EMBL:PDV99875.1};
OS   Candidatus Chloroploca asiatica.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Candidatus Chloroploca.
OX   NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDV99875.1, ECO:0000313|Proteomes:UP000220922};
RN   [1] {ECO:0000313|EMBL:PDV99875.1, ECO:0000313|Proteomes:UP000220922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7-9 {ECO:0000313|EMBL:PDV99875.1,
RC   ECO:0000313|Proteomes:UP000220922};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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:PDV99875.1}.
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DR   EMBL; LYXE01000063; PDV99875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3L0N8; -.
DR   OrthoDB; 9778581at2; -.
DR   Proteomes; UP000220922; 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; 1.
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; 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; 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:UP000220922}.
FT   DOMAIN          6..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          233..381
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   545 AA;  59485 MW;  C80963638DB05F0E CRC64;
     MTTLDTDTLE MVLTTLRDYA DRQLKPEFLR ELDERDEFPH EVLKDLYDPE KFGLHLIFIP
     EEFGGLGGGA YDIYRVSEQM ARIDLGVATG VLATFLGTDP IVVGGTDEQK ALWMGRIAEE
     GLLVAYGATE PQAGSDLGSL TTRATPVYED GQLTGYKISG RKQWISNGGV ATLYTILANT
     EGGPTWFVVE RGAPGFSWGK PEDKHGIRAS NTAALFLDEV FVPVENLVGG VEGQGLAQAQ
     AVFGYTRLMV AAFGLGGGWS ALERAIQYGQ TRIQGGALLA TKQAYTHKLL VPNAVRLEAA
     RAYIEWVAEN IDAGDPGQQT EGAVAKYFAT ESGNKAAEDA IQAHGGYGYT KEYMVEKVKR
     DVRITCIYEG TSEIMEWTIA RDRWQLHLKT RGAYYNDWAA KLEQLARANP DTGAATTALA
     LRALAVVLER CRIDRLTRNQ HILFRLGELI AWAETAAIFS ERAATHPSHA VPFSPETLRI
     MARIHAREAA LKVATDGLRW CISAGQTDPN LAGSLGLPAI YQAQAGQIED MNIVAERLNA
     AFPAE
//
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