ID A0A0S2I1L1_9BACT Unreviewed; 574 AA.
AC A0A0S2I1L1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ALO16162.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:ALO16162.1};
GN Name=mmgC_3 {ECO:0000313|EMBL:ALO16162.1};
GN ORFNames=L21SP5_02538 {ECO:0000313|EMBL:ALO16162.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO16162.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO16162.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO16162.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-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}.
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DR EMBL; CP013118; ALO16162.1; -; Genomic_DNA.
DR RefSeq; WP_057953557.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2I1L1; -.
DR STRING; 1307839.L21SP5_02538; -.
DR KEGG; blq:L21SP5_02538; -.
DR PATRIC; fig|1307839.3.peg.2665; -.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000064893; Chromosome.
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; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 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; IPR020964; Acyl-CoA_dehydrogenase_C.
DR InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 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 Pfam; PF12186; AcylCoA_dehyd_C; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF158494; PG0775 C-terminal 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893}.
FT DOMAIN 56..168
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 172..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 452..566
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12186"
SQ SEQUENCE 574 AA; 64919 MW; 0C7739172B5F6972 CRC64;
MANFYTDNKD LKFHLEHPLM KKIVDLKEHN YADHEKFDYA PADFEDALDN YNKVLEIVGD
ICANTIGPNA ESVDQDGPKV VDGRVEYARG TAENHEALTK AGLIGMSLPR KYKGLNFSMV
PYVMAAELVS RADAGFANIW GLQDCAETIH EFASDDLKDK YLPMFNEGAT AAMDLTEPDA
GSDLQAVQLK ATYNEQEDQW YLNGVKRFIT NGDADVSLVL ARSEAGTVDG RGLSLFLYDK
EDHAVNVRRI ENKLGIKGSP TCELVFNNAP AKLIGTRKMG LIKYVMSLMN GARLGVGAQS
VGIAEAAYRE ALEYAAERAQ FGKTIDKFPA VYEMLTNMEA RVKAVRALLY ETTRFVDVYK
AYTHLSEERK LEKEERQEMK HYTRLSDAFT PLLKLISSEY SNQIAYDSLQ IHGGSGFMKD
YPIERIYRDA RITTIYEGTS QLQVVAAIRG VTTGLFLKQI RAYEETAIKP EYEHLKRRLM
EMTAEYENVV SIVEEVNEQA EEDDYIDLQA RRMVEMAGNI IMGWLLLLDT MRDESYAQST
KVFLKMAYAE NAEKAAYIKN FEIEDMGMFK IHSD
//
