ID U2FUS3_9GAMM Unreviewed; 551 AA.
AC U2FUS3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Acyl-CoA dehydrogenase protein {ECO:0000313|EMBL:ERJ18078.1};
DE EC=1.3.8.7 {ECO:0000313|EMBL:ERJ18078.1};
GN ORFNames=SSPSH_003160 {ECO:0000313|EMBL:ERJ18078.1};
OS Salinisphaera shabanensis E1L3A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ18078.1, ECO:0000313|Proteomes:UP000006242};
RN [1] {ECO:0000313|EMBL:ERJ18078.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18078.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=21705588; DOI=10.1128/JB.05459-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT the harsh, variable environment of the brine-seawater interface of the
RT Shaban Deep in the Red Sea.";
RL J. Bacteriol. 193:4555-4556(2011).
RN [2] {ECO:0000313|EMBL:ERJ18078.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18078.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
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:ERJ18078.1}.
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DR EMBL; AFNV02000024; ERJ18078.1; -; Genomic_DNA.
DR RefSeq; WP_006913598.1; NZ_AFNV02000024.1.
DR AlphaFoldDB; U2FUS3; -.
DR STRING; 1033802.SSPSH_003160; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000006242; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; PS00072; ACYL_COA_DH_1; 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:ERJ18078.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006242}.
FT DOMAIN 19..173
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 187..280
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 291..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 60351 MW; 7B0EAA23F16AC719 CRC64;
MSDTHRAPRQ HLRTHDVTNQ PPPLEHYNAF TSDTALMEAV RREGGDWGQD RLKTYGAIAG
TELIEIGFEA NENRPELTTF DRYGHRIDEV RFHPAYHRSM TLAKEHGLHG LTWTAQREGA
QVVRSALFYM HNQMEAGTMC PITMTHASVP ALRHAPDVAA QWLPGILANS YDPTVAPHGD
KHGLTIGMGM TEKQGGSDVR ANTTRATARA DGSFGLVGHK WFFSAPMCDA FLVLAQEEAG
LSCFLLPRWT AAGKRNAIEI QRLKNKLGDH ANASSEVEFF DAEAYRVGDA GRGVPTIIEM
VSQTRLDCML GSAGLMRQAL VQAIHHCRYR EAFGARLIEQ PLMQHVLADM ALESEAAMAY
ALRVARAFES GDEHEKLLAR IATPVGKYLI CKAAPPLVNE AQECLGGAGY VEESIVPRLF
RQSPLNSIWE GSGNVQCLDM LRAMAKSPTA VEALHKELAV AQGAHPAYDR HCHDLQKMLG
AVADEPTQAR RVAEAVARAL QAKILLTGES SWVGEAFCEA RLSGNRGMAY GTLDTDLDFA
RIIARAGVAL D
//
