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Database: UniProt
Entry: A0A0L7T5M2_9GAMM
LinkDB: A0A0L7T5M2_9GAMM
Original site: A0A0L7T5M2_9GAMM 
ID   A0A0L7T5M2_9GAMM        Unreviewed;       542 AA.
AC   A0A0L7T5M2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Isovaleryl-CoA dehydrogenase {ECO:0000313|EMBL:KOC90692.1};
GN   ORFNames=NG42_08270 {ECO:0000313|EMBL:KOC90692.1}, NG43_12125
GN   {ECO:0000313|EMBL:KOC93116.1};
OS   Winslowiella iniecta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Winslowiella.
OX   NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC90692.1, ECO:0000313|Proteomes:UP000037088};
RN   [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B120 {ECO:0000313|EMBL:KOC90692.1,
RC   ECO:0000313|Proteomes:UP000037088}, and B149
RC   {ECO:0000313|EMBL:KOC93116.1, ECO:0000313|Proteomes:UP000036851};
RX   PubMed=26198254;
RA   Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA   Tisserat N.A., Leach J.E.;
RT   "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT   noxia).";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC90692.1}.
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DR   EMBL; JRXE01000009; KOC90692.1; -; Genomic_DNA.
DR   EMBL; JRXF01000017; KOC93116.1; -; Genomic_DNA.
DR   RefSeq; WP_052898839.1; NZ_JRXF01000017.1.
DR   AlphaFoldDB; A0A0L7T5M2; -.
DR   STRING; 1560201.NG42_08270; -.
DR   PATRIC; fig|1560201.3.peg.1761; -.
DR   OrthoDB; 9771038at2; -.
DR   Proteomes; UP000036851; Unassembled WGS sequence.
DR   Proteomes; UP000037088; 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; 6.10.250.600; -; 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:SF3; ACYL-COA DEHYDROGENASE AIDB-RELATED; 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:UP000037088}.
FT   DOMAIN          10..166
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          181..279
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          289..443
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   542 AA;  60165 MW;  087F6DB911E2B921 CRC64;
     MTWNTHTVFN QPRPLSNSNL FLSDTPLREA LIREGAEWDS ELQASVGQQL GSAESLELGR
     LANAWPPELL RYNACGERLD EVRFHPAWHL LMQGLCANRV HNLCWQADAR VGAFVARAAR
     FIQHAQVEAG TLCPITMTFG AIPLLQQSLP AAFHHWLPGL LSDRYDAHLQ PGDQKRGLLI
     GMGMTEKQGG TDVLSNTTSA QPLASRGNGE AYRLTGHKWF FSVPQSDAHL VLAQSPGGLS
     CFFLPRLLPD GSRNAIRIER LKEKLGNRSN ASSEVEFCNA TGWLLGEEGD GVRQILKMGG
     YTRFDCALGS HGLMRRALSV ALYHAHQRQV MGKNLVDQPL MRQVLSAQAL QLEGQTALLL
     RLARAWSSPA DESERAFSRL FTPAAKYVIC KNGINFVGEA MEVLGGIGYC EENELPRLYR
     EMPVNSIWEG SGNVMCLDVL RVLAKQPGVM EMLNREFDAV KGVNRHFDSG WRQLKLRLRK
     PQEAQAREIT SLLLRLAEGA QLLKSLDPPL ADAWCRQMLD RRGTSTLSED NCARLLLRAT
     GG
//
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