GenomeNet

Database: UniProt
Entry: A0A0X3TKT2_9RHOB
LinkDB: A0A0X3TKT2_9RHOB
Original site: A0A0X3TKT2_9RHOB 
ID   A0A0X3TKT2_9RHOB        Unreviewed;       567 AA.
AC   A0A0X3TKT2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KUJ76397.1};
GN   ORFNames=AVO45_11395 {ECO:0000313|EMBL:KUJ76397.1};
OS   Ruegeria marisrubri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ76397.1, ECO:0000313|Proteomes:UP000053791};
RN   [1] {ECO:0000313|EMBL:KUJ76397.1, ECO:0000313|Proteomes:UP000053791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ76397.1,
RC   ECO:0000313|Proteomes:UP000053791};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KUJ76397.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LQBQ01000035; KUJ76397.1; -; Genomic_DNA.
DR   RefSeq; WP_068348194.1; NZ_LQBQ01000035.1.
DR   AlphaFoldDB; A0A0X3TKT2; -.
DR   STRING; 1685379.AVO45_11395; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000053791; Unassembled WGS sequence.
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; 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, 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:UP000053791}.
FT   DOMAIN          3..33
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          78..156
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          161..269
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          281..436
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          451..560
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   567 AA;  60384 MW;  067599FDC84A749E CRC64;
     MPYRAPISDY EFLFKNVVGF DQVAETERFA EASSDVVSAI LTEAGKMCEQ VMAPLQRPGD
     LEPARLENGV LRTSPGYAEG WNAIAEGGWI GMSGNPEYGG MGLPMAVTTA VNEMMSAACL
     SLQLAPLMSQ GQIEALEHHA SDEIKELYLP KLISGEWSGT MNLTEPQAGS DVGALSSKAE
     PNGDGTYSIT GQKIFISWGD NDFCENVCHL VLARLPDGAP GTRGISLFLV PKFIPDENGN
     PGVANDLKVV SLEHKMGLHG SPTCVMQYDG AKGWLVGQEH KGMAAMFTMM NNARLGVGGQ
     GVGVAEGAYQ HALAYALERK QGKTPSGTIV DHADVRRMLM EMKADVFASR AILLANAVAI
     DMAQATGDAD WAARAALLTP IAKAFGTETG IRVAETGVQV HGGMGFIEET GAAQYYRDVR
     VTAIYEGTNG IQAMDLVGRK MMDGGEAAAR LLDEIEAQAE GARATMPELA GPVWEATESL
     REATEWLTSQ DDMTERFAGA LPYLRAFARV LGGHFHLAAA LADPDGPRAK LARFYINALL
     PEHAGLLAQA QNGAKDLYAL SADELAV
//
DBGET integrated database retrieval system