ID H5X8S4_9PSEU Unreviewed; 402 AA.
AC H5X8S4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EHR52499.1};
GN ORFNames=SacmaDRAFT_4312 {ECO:0000313|EMBL:EHR52499.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR52499.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR52499.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR52499.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
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|RuleBase:RU362125}.
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DR EMBL; CM001439; EHR52499.1; -; Genomic_DNA.
DR RefSeq; WP_009155877.1; NZ_CM001439.1.
DR AlphaFoldDB; H5X8S4; -.
DR STRING; 882083.SacmaDRAFT_4312; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_6_11; -.
DR OrthoDB; 142556at2; -.
DR Proteomes; UP000004926; Chromosome.
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; 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 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:UP000004926}.
FT DOMAIN 131..226
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 243..394
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 59..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 43237 MW; E7D74CB250ABB9E2 CRC64;
MINLEVPKKA RALVNQARQA AAEVFRPISR KYDRAEHAYP TELDMLASLL DGLNSSGEGG
AGAAGVRRND DDKRNGNRNG GNLSTVLGAI EMCWGDVALL LSMPRQGLGN AAIASVANEE
QLKRFSGLWA AMAITEPGCG SDSAAITTTA TPDGDDYILN GEKIFVTSGE RADAVVVWAT
LDKSKGRAAI KSFVVEKGTP GFEVVRLEHK LGIRASDTAV LRFDNCRVPK QNLLGSPEID
TKSGFAGVMQ TFDNTRPLVA AMAIGVARAA LEETKRLLEE AGVKIDYDKP ANAQHAAAAA
YLQLEADYEA AYLLTLESAW MADNRKPNSL QASMAKAKAG RSVVDITLRC VELAGTLGYT
EELLLEKWSR DAKILDIFEG TQQIQQLIVA RRLLGKTSAE LK
//
