ID M0NRH7_9EURY Unreviewed; 406 AA.
AC M0NRH7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:EMA60203.1};
GN ORFNames=C469_09065 {ECO:0000313|EMBL:EMA60203.1};
OS Halorubrum lipolyticum DSM 21995.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227482 {ECO:0000313|EMBL:EMA60203.1, ECO:0000313|Proteomes:UP000011650};
RN [1] {ECO:0000313|EMBL:EMA60203.1, ECO:0000313|Proteomes:UP000011650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21995 {ECO:0000313|EMBL:EMA60203.1,
RC ECO:0000313|Proteomes:UP000011650};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA60203.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOJG01000025; EMA60203.1; -; Genomic_DNA.
DR RefSeq; WP_008005835.1; NZ_AOJG01000025.1.
DR AlphaFoldDB; M0NRH7; -.
DR STRING; 1227482.C469_09065; -.
DR PATRIC; fig|1227482.3.peg.1827; -.
DR OrthoDB; 275197at2157; -.
DR Proteomes; UP000011650; 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; 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.
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|RuleBase:RU362125}.
FT DOMAIN 12..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..227
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 239..386
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 406 AA; 44181 MW; B4DD509A6A728CC9 CRC64;
MEYDDVGRGP EVAAAVREFV DETVLPVERE WLGRGPIPSA EVEALREAAR DRGIYAPQVD
EAYGGLGLGF REMLPVFEEA GRSLLGPTAL RCAAPDEGNM HTFEIAATDD QKERWLRPLA
TGEIDSAFAM TEPMQGGGSD PKMLATTAEK AGDEWVIDGH KWWTTGGAEA DVFLTFARTD
PEAHPYAGCS VILVPADADG VEVVREIPHL GEGLAGTSHA EIRFDGVRVP VENTLGEENE
GFALVQRRLG PARLTHCMRY AGMADRALDV ATAYLAEREG FGEPLAEKQG PRFRIADRRT
ELHAARTVVR HAAGRIADGG EARVEVAMAK TFAANAVQEA IDDALQFCGG NGIGHDLPIA
RFYENVRQFR IVDGADEVHR RTIARDAFAD PPTEELDAVT RFGEFE
//
