(data stored in SCRATCH zone)

SWISSPROT: B4SSM1_STRM5

ID   B4SSM1_STRM5            Unreviewed;       387 AA.
AC   B4SSM1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACF49903.1};
GN   OrderedLocusNames=Smal_0198 {ECO:0000313|EMBL:ACF49903.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49903.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49903.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49903.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP001111; ACF49903.1; -; Genomic_DNA.
DR   RefSeq; WP_012509747.1; NC_011071.1.
DR   STRING; 391008.Smal_0198; -.
DR   EnsemblBacteria; ACF49903; ACF49903; Smal_0198.
DR   KEGG; smt:Smal_0198; -.
DR   eggNOG; ENOG4105C1G; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000131659; -.
DR   KO; K00253; -.
DR   OMA; NSLCTNH; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01000-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01156; IVD; 1.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
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.
DR   InterPro; IPR034183; IVD.
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; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SSM1.
DR   SWISS-2DPAGE; B4SSM1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN       13    122       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      127    222       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      234    382       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   387 AA;  41474 MW;  DF45044D1235A539 CRC64;
     MHVPSLNFDL GEDIDLLRQS VAHFAAAEVA PLAAEADATN QFPLALWPKL GEQGLLGLTV
     EEEYGGTGMG YLAHVVAMEE ISRASGGIGL SYGAHSNLCV NQLRKNGNEE QKQRFLPGLC
     SGALVGALAM SEPGAGSDVV SMKLRADKRG DRYVLNGNKM WITNGPDADV LVVYAKTDMA
     AGAKGITAFL VEKGMKGFST AQKLDKLGMR SSPTCELVFQ DCEVPEENVL GQVGGGVRVL
     MSGLDYERVV LSGGPLGLMA AAMDVVMPYV HERHQFGEAI GSFQLIQAKI ADMYVGLGAC
     RAYVYAVARA CDQGRTTRQD AAGAILYAAE KATWLTGQAI QILGGNGYIN EYPTGRLWRD
     AKLYEIGAGT SEIRRMLIGR ELFQRTL
//

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