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Database: UniProt
Entry: Q2N6I0_ERYLH
LinkDB: Q2N6I0_ERYLH
Original site: Q2N6I0_ERYLH 
ID   Q2N6I0_ERYLH            Unreviewed;       569 AA.
AC   Q2N6I0;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=Acyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:ABC64711.1};
GN   OrderedLocusNames=ELI_13095 {ECO:0000313|EMBL:ABC64711.1};
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC64711.1, ECO:0000313|Proteomes:UP000008808};
RN   [1] {ECO:0000313|Proteomes:UP000008808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808};
RX   PubMed=19168610; DOI=10.1128/JB.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
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}.
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DR   EMBL; CP000157; ABC64711.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2N6I0; -.
DR   STRING; 314225.ELI_13095; -.
DR   KEGG; eli:ELI_13095; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_12_2_5; -.
DR   Proteomes; UP000008808; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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   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, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008808}.
FT   DOMAIN          28..146
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          151..261
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          277..439
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          468..563
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   569 AA;  60631 MW;  118306024207DB68 CRC64;
     MLSIRVNAGI AELAKSERFA AAEPDMVEAI VEGVGQFAAG EFAPLNRVGD LEGAKLENGV
     VRLPNGFAEA YDQYVEQGWN AIASPAEFGG QGLPFTLACN VLENLGTANM AFNLLPMLSV
     GAIEAIEHHG SEAQQSRYLP KLVSGEWSGT MNLTEPQAGS DVGALRSTAV PITEGEHAGK
     YRVRGQKIYI TWGDHELAKN IIHLVLARTP DAPEGSRGIS LFLVPKYHVH DDASLGPRND
     LRPVSLEHKL GIHASPTCVM SYGDNDECIG ELVGAENRGL VAMFTMMNNA RINVGNQGVQ
     IGERATQQAL HYARDRIQSA RAGSPDKSPV AILEHPDVRR MLLRMKALTE GARALLYYTA
     GQVDRGTIGD EAAKARGEIL TPMIKAWGTD IGIEIASIGV QVHGGMGFVE ETGAAQHYRD
     ARIAPIYEGT NGIQAADLVT RKLGLEDGQA LIGLLEDIAR DAADEPKLFA LAGDCAAIAR
     WMREEASLDD RLAGSVPFTT MCAVAVAGWQ MLQQLRAVAA GASPALAETK PVTARFFLDR
     IVPEASGLKA SAIAGSDSLY ALPADKLIA
//
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