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Database: UniProt
Entry: L9WJD4_9EURY
LinkDB: L9WJD4_9EURY
Original site: L9WJD4_9EURY 
ID   L9WJD4_9EURY            Unreviewed;       369 AA.
AC   L9WJD4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ELY49346.1};
GN   ORFNames=C493_20786 {ECO:0000313|EMBL:ELY49346.1};
OS   Natronolimnohabitans innermongolicus JCM 12255.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronolimnohabitans.
OX   NCBI_TaxID=1227499 {ECO:0000313|EMBL:ELY49346.1, ECO:0000313|Proteomes:UP000011602};
RN   [1] {ECO:0000313|EMBL:ELY49346.1, ECO:0000313|Proteomes:UP000011602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12255 {ECO:0000313|EMBL:ELY49346.1,
RC   ECO:0000313|Proteomes:UP000011602};
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:ELY49346.1}.
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DR   EMBL; AOHZ01000096; ELY49346.1; -; Genomic_DNA.
DR   AlphaFoldDB; L9WJD4; -.
DR   STRING; 1227499.C493_20786; -.
DR   eggNOG; arCOG01707; Archaea.
DR   Proteomes; UP000011602; 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   CDD; cd00567; ACAD; 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; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000011602}.
FT   DOMAIN          3..85
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          114..202
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          246..342
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   369 AA;  40672 MW;  9F6B0A9415940E2C CRC64;
     MITDEREMIR DSVREVMDEE IAPDLAEADR EPLSKDDVID YMQRTAEIDV GPYAEERFDD
     PLAGTIVSEE VSRVWPSLQV TKGMSLPVTM FEIFSERTRE SCAEEYENDR LVGCFAITEP
     EGGSDTKVPN TTATKDGDEY VITGEKTWVS NAPIADVALV VARDEDAERR DMFLVDEKTA
     GFDARELEKL GWKGAPTGQL FFGEARVPRE NKLSRAVMEP ISDGRMDPNE SSFATGGGVG
     GNPLNTMFAS MRNGMAAISV RIMQAAYEAA LEYATDREVF DQPIGQHQLV QEKRYNIRAG
     LETGRLLTRY TAQKIAAGDL EARMLSSLSK GWVCEKSVEV TSTPCRSTAA IASRRTTRSS
     ATTATTGRG
//
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