ID D5VG89_CAUST Unreviewed; 414 AA.
AC D5VG89;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Acyl-CoA dehydrogenase type 2 domain protein {ECO:0000313|EMBL:ADG10208.1};
GN OrderedLocusNames=Cseg_1728 {ECO:0000313|EMBL:ADG10208.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG10208.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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DR EMBL; CP002008; ADG10208.1; -; Genomic_DNA.
DR RefSeq; WP_013078865.1; NC_014100.1.
DR AlphaFoldDB; D5VG89; -.
DR STRING; 509190.Cseg_1728; -.
DR KEGG; cse:Cseg_1728; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_2_0_5; -.
DR Proteomes; UP000002629; 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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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 Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
FT DOMAIN 39..125
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 259..393
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 45129 MW; 04A0A288EB2705C7 CRC64;
MIAEMRGQRP NPTISAISPP EPDLTPDQMI ARADGMRDLL RERQAAAEAA GNISQETNQA
MVDAGFYRVI QPRTFGGYGF DLPTYVRLVT AVARGCPETA WVLSLVLGHV HQLATYSLEA
QIEAYGETGD FRAPEVAAPQ GRGIPVPGGF SVTGAWDYAS GCAHATHILL TFLVTDPQSG
ATTMRMGLFH RSEYEIVRNW EVIGMQGTGS DRVVMTDVFV PDYRAKPYPP FDAVPPAEAY
AESPLFYGPA RPFIVTESAS VIVGAAEGAL DLYEESFRAR KATGPTGAPR QELAEYQLNY
GRCRALVDTA RAALLQTATD YMEIARRTHE TGQPCSEEVF RRLTLVILQS IHLAHEAVDI
IFRTAGTAAS KKDAMLGRYW RNVGVLRGHL AHQSDSASIN YGRTHFGQPP VGIA
//
