ID J3HHW2_9BURK Unreviewed; 596 AA.
AC J3HHW2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EJM96085.1};
GN ORFNames=PMI40_04754 {ECO:0000313|EMBL:EJM96085.1};
OS Herbaspirillum sp. YR522.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJM96085.1, ECO:0000313|Proteomes:UP000007507};
RN [1] {ECO:0000313|EMBL:EJM96085.1, ECO:0000313|Proteomes:UP000007507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR522 {ECO:0000313|EMBL:EJM96085.1,
RC ECO:0000313|Proteomes:UP000007507};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM96085.1}.
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DR EMBL; AKJA01000154; EJM96085.1; -; Genomic_DNA.
DR RefSeq; WP_008119844.1; NZ_AKJA01000154.1.
DR AlphaFoldDB; J3HHW2; -.
DR STRING; 1144342.PMI40_04754; -.
DR PATRIC; fig|1144342.3.peg.4306; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000007507; 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; 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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_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 Reference proteome {ECO:0000313|Proteomes:UP000007507}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 82..160
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 165..273
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 285..452
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 471..592
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 596 AA; 65292 MW; 886476165FB75270 CRC64;
MPQYQAPIRD MQFVLHELLN VEEVLKDLPP HADTNRELID QVLEEGGKFT SQVLFPLNHP
GDREGCHFDR ETHSVTTPKG FKEAYRQYIE AGWPALACDT EYGGQGLPLV LNNSFYEMLN
SSNQAWTMYP GLSHGAYECL HAHGSDEQKK LYLPKLVSGE WTGTMCLTEA HCGTDLGLLR
SKAEPQADGS YKITGNKIFI SAGENDMSAN IVHLVLARLP DSPQGSKGIS LFIVPKFLPQ
ADGSLGGRNP VTCGAIEEKM GIHGNATCQI NLDGATGWLI GQPHKGLQAM FVFMNAARLG
VGMQGLGLTE VAYQNAVTYA KDRVQMRSLS GIKAPEKAAD PIIVHPDVRR MLLTARAYAE
GGRAFCSYVA LELDRELSHP DEQVRRDAGD IVALLTPVVK AFLTDNAWSA TSECLQVYGG
HGYISEWGME QYVRDARINM IYEGTNTIQS LDLLGRKVLM DNGAKLKKFG ALIQAFVEEH
GTDEAMSEFI TPLADIGDKV SKLTMEIGMK SFANQDEAGA AAVPYLRVVG HLVFAWLFAR
SASIALAKQD SGDSFYTAKL ATARFYFARL LPETAMLIRQ ARSGSANLMA LDADLF
//
