ID R4Z6D5_9ACTN Unreviewed; 426 AA.
AC R4Z6D5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CCM64442.1};
DE EC=1.3.8.- {ECO:0000313|EMBL:CCM64442.1};
GN ORFNames=BN381_40056 {ECO:0000313|EMBL:CCM64442.1};
OS Candidatus Microthrix parvicella RN1.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Microthrixaceae; Microthrix.
OX NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM64442.1, ECO:0000313|Proteomes:UP000018291};
RN [1] {ECO:0000313|EMBL:CCM64442.1, ECO:0000313|Proteomes:UP000018291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN1 {ECO:0000313|EMBL:CCM64442.1,
RC ECO:0000313|Proteomes:UP000018291};
RX PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT based on genomic and metagenomic analyses.";
RL ISME J. 7:1161-1172(2013).
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:CCM64442.1}.
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DR EMBL; CANL01000034; CCM64442.1; -; Genomic_DNA.
DR RefSeq; WP_012228544.1; NZ_HG422565.1.
DR AlphaFoldDB; R4Z6D5; -.
DR STRING; 1229780.BN381_40056; -.
DR GeneID; 78311863; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_1_0_11; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000018291; 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; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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.
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|RuleBase:RU362125,
KW ECO:0000313|EMBL:CCM64442.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018291}.
FT DOMAIN 15..129
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 133..202
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..375
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 426 AA; 47693 MW; 6904CC857F5CF91F CRC64;
MAWDFSTEPE FQKKLDWVER FCREQVEPLD LVFPYAVRSK DPKLKALVKD LQDQVKEQGL
WALFLDEDLG GPGFGQLKLG LLNEILGRYG SAPQIFGAGA PDTGNMEMLA AYGTDDQKER
WLTPMLNQEL WSAYSMTEPQ GGSDPNLFTT HAVKDGDEWV INGEKWFTSA GRVADLLFVM
CTNGMFVVPR KTPGVEIMPE PRNHNHIVYT DVRVPADHLL GPEDGAKVLA QRRLGGGRIH
HAMRTISQCT LAFDMMCERA LSRESHGKII GDHQMVQEKI ADSYASIRML RLFVLETAWK
IDNTSTQEAR TDIAAVKFTM AKVLREVSFN ALHILGSLGT TNLTPLQAMY ASAPTMGIAD
GVDEVHKATV ARNVLKGYRP HEGFWPTEYL PAKRAAARER FEPMFAADPE LRDRADAYAK
YLATKG
//
