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Database: UniProt
Entry: A0A0J6FSC7_9BACI
LinkDB: A0A0J6FSC7_9BACI
Original site: A0A0J6FSC7_9BACI 
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
//
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