GenomeNet

Database: UniProt
Entry: Q21E48_SACD2
LinkDB: Q21E48_SACD2
Original site: Q21E48_SACD2 
ID   Q21E48_SACD2            Unreviewed;       394 AA.
AC   Q21E48;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Histidine kinase {ECO:0000313|EMBL:ABD83031.1};
DE            EC=2.7.3.- {ECO:0000313|EMBL:ABD83031.1};
GN   OrderedLocusNames=Sde_3776 {ECO:0000313|EMBL:ABD83031.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD83031.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD83031.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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   ---------------------------------------------------------------------------
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; CP000282; ABD83031.1; -; Genomic_DNA.
DR   RefSeq; WP_011470246.1; NC_007912.1.
DR   AlphaFoldDB; Q21E48; -.
DR   STRING; 203122.Sde_3776; -.
DR   KEGG; sde:Sde_3776; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_699982_0_0_6; -.
DR   OrthoDB; 6138585at2; -.
DR   Proteomes; UP000001947; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00567; ACAD; 1.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF42; SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125}; Kinase {ECO:0000313|EMBL:ABD83031.1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW   Transferase {ECO:0000313|EMBL:ABD83031.1}.
FT   DOMAIN          22..123
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          129..222
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          299..391
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   394 AA;  42747 MW;  E05C389862DAD917 CRC64;
     MLNCELTPSF WRNDAFIHLR KQIDTSFAAH LTPASNSESV NFQALVRQLY NDNLSGLRYA
     KNKGGTGHGL AAQALFAESL GRVPSGGIGM GLTIHLDMVA PIVDQQGSAH QLEEYLLPAL
     RGDIIFSHAV SEPHAGSDIS NIQTTAVKDG DGWRIDGCKS MIALASLADV HFVVARIPGH
     KPPFNKINFL IPAATTGVKV SSATPTLGNN DCPIANITFD NVWVADSNRL GTAGMGMIHQ
     MQQFSQERIL SSLRANEVAR MCLAHAEHLL TKPNNLNTLN NRHNTPNPNT ASCVNSLNKL
     HTLKAQLNAS KAITYKAMGR WIDNGDYHTL SCSSKLLSSR LVRQASILAL TASKTLGEES
     DAQLVHYFND ARLYSISTGS DEMMLKSIAA SEKY
//
DBGET integrated database retrieval system