ID A0A1H4BF35_ALKAM Unreviewed; 822 AA.
AC A0A1H4BF35;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000256|ARBA:ARBA00020144};
DE EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033};
DE EC=1.3.8.8 {ECO:0000256|ARBA:ARBA00012040};
GN ORFNames=SAMN04488051_103313 {ECO:0000313|EMBL:SEA46412.1};
OS Alkalimonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alkalimonas.
OX NCBI_TaxID=152573 {ECO:0000313|EMBL:SEA46412.1, ECO:0000313|Proteomes:UP000198773};
RN [1] {ECO:0000313|EMBL:SEA46412.1, ECO:0000313|Proteomes:UP000198773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3430 {ECO:0000313|EMBL:SEA46412.1,
RC ECO:0000313|Proteomes:UP000198773};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000256|ARBA:ARBA00034035};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; FNRM01000003; SEA46412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4BF35; -.
DR STRING; 152573.SAMN04488051_103313; -.
DR OrthoDB; 9802447at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000198773; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:InterPro.
DR CDD; cd00567; ACAD; 1.
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; 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 InterPro; IPR047634; FadE.
DR InterPro; IPR015396; FadE_C.
DR NCBIfam; NF038187; FadE_coli; 1.
DR PANTHER; PTHR48083:SF18; ACYL-COENZYME A DEHYDROGENASE; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF09317; ACDH_C; 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000198773}.
FT DOMAIN 134..233
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 238..328
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 361..508
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 515..797
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
SQ SEQUENCE 822 AA; 90222 MW; DB8441B4F30D8FFD CRC64;
MEGFVFSLIL LVVIGILAYY RASLTLFTAA IAVTLAAGTV AGPVGLASWI VFLLIALPLN
VAFIRQKLLT QPLLGVYRKI MPEMSSTEKE AIDAGTTWWE ADLFRGNPDW QKLHNFPIPR
LSAEEQAFLD GPVEELLDMV DDWEITHDRA DLSPEVYQYL KDKGFFAMII KKQYGGLEFS
AYAQSCVLQK LTSKSMVLSS IVGVPNSLGP GELLQHYGTE EQKNHYLPRL AKGLDVPCFA
LTSPEAGSDA GSIPDYGIVC KGQWQGKEVL GMRLTWNKRY ITLAPIATVL GLAFKLQDPD
KLLGDKEDLG ITCALIPADT PGVKIGRRHF PLNVPFQNGP TQGNDVFVPL DYIIGGAKMA
GQGWRMLVEC LSVGRAITLP SNSTAGIKAA AMSTGAYARI RRQFKIPIGK MEGVEEALAR
IGGSAYMACA STTMSVGSID LGEKPSVISA ITKYHITERM RLAMIDAMDV HGGKGICMGP
NNYLARGYQG APVAITVEGA NILTRNMIIY GQGAIRCHPY VLAELQAAYN EDNRAAVTAF
DKALFGHIGF AISNFFRTFW LSLTGAAFSS APYNDATAKY YKQMNRFSAA LALMSDVAMG
TLGGDLKRRE RISARLGDIL SMLYLTSSVL KRFQDEGRQP QDLPLVQWAC EDNLSKAQLA
LDELFDNFPN RLVGVVLKRV VFPWGRTLRR PSDTVEHQVA RIMQTPCEAR SRLGHHLYLA
GKDNNPIGMV EQALRDVLAA EPLFDKVTEA AKKRLPFFRL NEVADLGLEL KVISEQEAQV
LRQAEASRLR TINVDDFDFN YLAADKALLA SEQQSSAKVN AA
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