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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//