ID A0A0J6FSC7_9BACI Unreviewed; 559 AA.
AC A0A0J6FSC7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Isovaleryl-CoA dehydrogenase {ECO:0000313|EMBL:KMM37237.1};
GN ORFNames=AB986_15340 {ECO:0000313|EMBL:KMM37237.1};
OS Alkalihalobacillus macyae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM37237.1, ECO:0000313|Proteomes:UP000035996};
RN [1] {ECO:0000313|EMBL:KMM37237.1, ECO:0000313|Proteomes:UP000035996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM37237.1,
RC ECO:0000313|Proteomes:UP000035996};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMM37237.1}.
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DR EMBL; LELK01000004; KMM37237.1; -; Genomic_DNA.
DR RefSeq; WP_048312109.1; NZ_LELK01000004.1.
DR AlphaFoldDB; A0A0J6FSC7; -.
DR STRING; 157733.AB986_15340; -.
DR PATRIC; fig|157733.3.peg.1142; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000035996; 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; 2.40.110.20; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035996}.
FT DOMAIN 2..154
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 165..263
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 275..428
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 559 AA; 63152 MW; CA95B5C8A3B7E2CF CRC64;
MRNFYTEDPN LATLLKAYLE PGFFQWAEEE LVEYGALCAN EIDDRARHTD REGQPKLLKY
DKMGNDISFV WKNEGYLKTV KQTYDRGIVG YVHKEIPALG HKGNYIYSFA QGYLLSQSEP
GFYCPVTLTM ATAYLIDHYA DEKLKEKFLP HVLATGDVEL YEGATFLTER QGGSDVGANE
TRAVKEGENY LLTGEKYFAS NAGACGVAMV LARIDDQKQG TKGLSLFLVP WKKDDGSNNN
LSIRRLKDKL GVKAVPSAEV LLEGSKAYLV GDASKGFSYM AEALNLSRLC NAVASVGIMQ
RAYLEAKSYA YERGAFKQKL KDFPMIRESL VNMKVKHEVE MSALFSSIAL FEKVASGQSS
EEEQALNRLL IALVKKETAE QAVHFSHEAI EMHGGNGYIE DFVTPRLLRD AQVLTVWEGT
ANILGLEVLR LIHKYEVHHL FFARMKRELD NLPENLALEK TKVMKAIDSA HARINQISQM
NQSMQTYHSK RMTKWLTNIF ESTIALKDAA QYGERKQAIS RIFIEHTLQS DPYLLSELAL
KHYELIVEKT PVSSELQRN
//