ID A0A1R4K3J4_9SPHI Unreviewed; 401 AA.
AC A0A1R4K3J4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acyl-CoA dehydrogenase, short-chain specific {ECO:0000313|EMBL:SJN38764.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:SJN38764.1};
GN ORFNames=FM107_09780 {ECO:0000313|EMBL:SJN38764.1};
OS Sphingobacterium sp. JB170.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1434842 {ECO:0000313|EMBL:SJN38764.1, ECO:0000313|Proteomes:UP000195951};
RN [1] {ECO:0000313|EMBL:SJN38764.1, ECO:0000313|Proteomes:UP000195951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB170 {ECO:0000313|EMBL:SJN38764.1,
RC ECO:0000313|Proteomes:UP000195951};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 ---------------------------------------------------------------------------
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; FUKU01000030; SJN38764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4K3J4; -.
DR OrthoDB; 1522475at2; -.
DR Proteomes; UP000195951; Unassembled WGS sequence.
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:SF42; SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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|RuleBase:RU362125,
KW ECO:0000313|EMBL:SJN38764.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195951}.
FT DOMAIN 7..120
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 124..218
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 230..376
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 401 AA; 45183 MW; 7B5C7E715DA7544C CRC64;
MHATQLTEEH QEFREILQAF IRKEILPNTD TWEKEGQIDR AIWKKMGAMG FMGINYPQAY
GGVELDFYYA MIFCEEISKC YSGGFSIATL VIQFMSAPYL LKHASESLKQ RYLTPVISGD
LVSAIAITEP GAGSDIKNIK TYAERVDDHF IVNGSKTFIT NGFYGDYFIT AVKTHKGDKN
REITLLLIDR NAQGVHSSKI KKMGLYASDT AELAFINVKV PIYNVIGEEG EGFNYLMDGL
QLERLITAIY SLSMADSALQ YTLSYVQSRE AFGSRIQEFQ AIRHRIAQMV ADVESCRAYI
YHCADLQQKE TYAVKECSIA KLQSSELAIK IVHQCLQLFG GYGYTEDYKI ARLYRDVRVG
TIIAGTSEIM LEIIAKMEID RIKYESKPKS RSLGNSGAPS T
//
