ID F8DC90_HALXS Unreviewed; 383 AA.
AC F8DC90;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:AEH37210.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:AEH37210.1};
GN OrderedLocusNames=Halxa_2592 {ECO:0000313|EMBL:AEH37210.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH37210.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|EMBL:AEH37210.1, ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(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|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CP002839; AEH37210.1; -; Genomic_DNA.
DR RefSeq; WP_013880100.1; NC_015666.1.
DR AlphaFoldDB; F8DC90; -.
DR STRING; 797210.Halxa_2592; -.
DR GeneID; 10797547; -.
DR KEGG; hxa:Halxa_2592; -.
DR eggNOG; arCOG01707; Archaea.
DR HOGENOM; CLU_018204_3_5_2; -.
DR OrthoDB; 275197at2157; -.
DR Proteomes; UP000006794; Chromosome.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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 PIRSF; PIRSF016578; HsaA; 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:UP000006794}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..218
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 235..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 383 AA; 42143 MW; AF017C0C79AC49FE CRC64;
MEFGLTDEQR QIREEIQRFA ENEIVPHAAE YDREEKFPRD IVDEAAEMGL TGAHIPMEYG
GAGYSILDTA IITEELFSYD PGIALSIVST SFGCEAIMNF GTEDQKERFL EPVAAGEKIS
GAAISEPDTG SDVSSVSTRA EKDGDEWVIN GNKMWITNGS VGDFFVVLCK TDPDAEGRYN
GFSQIVVESD RDGFEAEKIS GKLGIRASDT AELVFDDVRV PEENLIGTRD AAFMQQMQFF
DETRVAVAAQ GVGIAKGATR AALEYAQDRE QFGKSISEFQ AIQHKLAEMA TDTEAARNLT
YKAAWNVDQG EDITKLASMA KEYASRVAVD VADEAVQIHG GAGYVDDFPV ERFYRDAKIT
QIYEGTTEIQ KNVIAREMLG KGF
//