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Database: UniProt
Entry: A0A013VN14_9SPHN
LinkDB: A0A013VN14_9SPHN
Original site: A0A013VN14_9SPHN 
ID   A0A013VN14_9SPHN        Unreviewed;       736 AA.
AC   A0A013VN14;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EXS69892.1};
GN   ORFNames=BF95_12045 {ECO:0000313|EMBL:EXS69892.1};
OS   Sphingobium sp. Ant17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS69892.1, ECO:0000313|Proteomes:UP000021537};
RN   [1] {ECO:0000313|EMBL:EXS69892.1, ECO:0000313|Proteomes:UP000021537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ant17 {ECO:0000313|EMBL:EXS69892.1,
RC   ECO:0000313|Proteomes:UP000021537};
RA   Adriaenssens E.M., Cowan D.A.;
RT   "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT   Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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:EXS69892.1}.
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DR   EMBL; JEMV01000026; EXS69892.1; -; Genomic_DNA.
DR   RefSeq; WP_043151819.1; NZ_JEMV01000026.1.
DR   AlphaFoldDB; A0A013VN14; -.
DR   STRING; 1461752.BF95_12045; -.
DR   PATRIC; fig|1461752.3.peg.2890; -.
DR   OrthoDB; 7795946at2; -.
DR   Proteomes; UP000021537; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 2.
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; 2.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          6..103
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          202..335
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          358..469
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          474..553
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          601..728
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   736 AA;  79031 MW;  961498154463BD83 CRC64;
     MNFDLTDDQE MMRDMFVRFM DEHSSIARVR AAAPSGFDPA LWTGLAELGA LSIRVPEEAG
     GLGLGLFDAV LLMEEAGRTL VSGPLAETLV AARMLALLGG DAATALLGRV MAGEAVASIA
     FHDIATQPVQ WIGGGQVAQA VVARRGDDIV LIDVQDGARV AEENLADTPM AHIDLGALPQ
     VVLASSADAV ATFASGVEEW KLLVAAGLAG IGREALKLAA AYACERKQFD QFIGQFQGIS
     HPLADLLCDV DGGKFLVWKA IRDIADGAPE AGAAISIAAW WNSDAAGRAV AQALHTFGGY
     GLTTEYDIFL FNLRAKAWPL LLGDPQRLIT EAGRRLFAGE QAALPDAGDM PVNFDLGDDA
     RAITQEIEDF FAAHVTPEMR EAFHYSWEGY NPDLNRKLAA QNLLYLGLPQ DVGGRGLSAY
     EKTAAMDAFE AEGYNNPAAN VTQMVALIVH RFGSEELKAA ILPEIMRGEV ICSLGYSEPG
     AGSDVFAAQC RATQEADGSW RIDGTKMFTS GANLSTYVLM LCRTNPDVAK HKGLTMFIVP
     LKAEGVTIQP VHTFQDERTN ITFYDGVKIP DSWRLGAVDG GVRTMSASLE LEHGGGFAKY
     QRAMLHAAET LCQEIQRDGQ PLIADAGAQA RLARTAANLW ASELIAFRAN WASMEKKPNL
     AYGPMAKMFS SEKFQSDARD LMDLTAPLSL SKRKGAAAEI NMFYRHAQGA TIYGGTSEVH
     RSMIAERALG LPRTRA
//
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