UniProt: A0A0H4VVE9

Database: UniProt
Entry: A0A0H4VVE9_9BORD

LinkDB:  A0A0H4VVE9_9BORD 
Original site:  A0A0H4VVE9_9BORD

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Ontology (2)   
   GO (2)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (10)   
   InterPro (7)   
   Pfam (3)   
Literature (2)   
   PubMed (2)   
All databases (18)   

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ID   A0A0H4VVE9_9BORD        Unreviewed;       401 AA.
AC   A0A0H4VVE9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AKQ53950.1, ECO:0000313|EMBL:AZW16241.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:AKQ53950.1};
GN   ORFNames=ACR54_00598 {ECO:0000313|EMBL:AKQ53950.1}, CS347_05355
GN   {ECO:0000313|EMBL:AZW16241.1};
OS   Bordetella hinzii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ53950.1, ECO:0000313|Proteomes:UP000036382};
RN   [1] {ECO:0000313|EMBL:AKQ53950.1, ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|EMBL:AKQ53950.1,
RC   ECO:0000313|Proteomes:UP000036382};
RX   PubMed=26316634;
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT   Humans.";
RL   Genome Announc. 3:e00965-e00915(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA   Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000282741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA   Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA   Williams M.M.;
RT   "Whole genome sequencing of various Bordetella species.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AZW16241.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H720 {ECO:0000313|EMBL:AZW16241.1};
RX   PubMed=31744907;
RA   Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA   Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA   Unoarumhi Y., Williams M.M., Tondella M.L.;
RT   "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT   Bordetella Respiratory Pathogens.";
RL   mSystems 4:e00702-19(2019).
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}.
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DR   EMBL; CP012076; AKQ53950.1; -; Genomic_DNA.
DR   EMBL; CP024172; AZW16241.1; -; Genomic_DNA.
DR   RefSeq; WP_029578183.1; NZ_LT906461.1.
DR   STRING; 103855.ACR54_00598; -.
DR   KEGG; bhz:ACR54_00598; -.
DR   PATRIC; fig|103855.14.peg.528; -.
DR   eggNOG; COG1960; Bacteria.
DR   Proteomes; UP000036382; Chromosome.
DR   Proteomes; UP000282741; Chromosome.
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; 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   PANTHER; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AKQ53950.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036382}.
FT   DOMAIN          20..128
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          133..227
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          240..393
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   401 AA;  43985 MW;  E25FF0B6C08706C3 CRC64;
     MHFDQHVAVP DPAAGPEVYR QHARAWLRAN LPDFMRSDSL DWRAPTLAES SAWEAAMYQA
     GLAGMTWPKP YGGHGLSLRE HLAVNKEVGA LPMPESVSSI GKELAGPIIM AVGTEAQKQA
     FLPNILSMKQ YWCQGFSEPD AGSDLARLRT KAVQEGGHWR INGQKIWTSG AAKAHYCLLL
     TRTGTVADKH RGLLMFAVPM DTPGIRVVPI KSIDGKSSFA EVFFDDVVVP DSARLGAPDE
     GWSAAIRVLS IERATNRMYR PWRFECELRQ LIAACKSDSQ LASALDDGYV QRRIGDLVGE
     IDGLKGLVEL TVERMMRGES IGARGSLTKL YWSECHQAFA GLALSLLSQV GPHSSPLARR
     AHAAFTNAYL FARAETIYAG TTEVQLDVIA QRIMNLPKDL T
//

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