(data stored in SCRATCH zone)

SWISSPROT: B8IAU0_METNO

ID   B8IAU0_METNO            Unreviewed;       391 AA.
AC   B8IAU0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACL55333.1};
GN   OrderedLocusNames=Mnod_0289 {ECO:0000313|EMBL:ACL55333.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55333.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55333.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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; CP001349; ACL55333.1; -; Genomic_DNA.
DR   RefSeq; WP_015927045.1; NC_011894.1.
DR   STRING; 460265.Mnod_0289; -.
DR   EnsemblBacteria; ACL55333; ACL55333; Mnod_0289.
DR   KEGG; mno:Mnod_0289; -.
DR   eggNOG; ENOG4105C1G; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000131659; -.
DR   KO; K00253; -.
DR   OMA; TFPRDLW; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; MNOD460265:GCZK-291-MONOMER; -.
DR   Proteomes; UP000008207; 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; B8IAU0.
DR   SWISS-2DPAGE; B8IAU0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT   DOMAIN       15    126       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      130    225       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      237    385       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   391 AA;  42364 MW;  165C46D1741D36EE CRC64;
     MIPNAAREFN FGLGETADAI RESVRDFARD RIAPRAEEID RTNTFPRDLW PEMGALGLHG
     ITVEEEYGGL GLGYLEHCVA MEEVSRASAS VGLSYGAHSN LCINQIRRNG SDAQKRRYLP
     KLISGDEVGA LAMSEPGSGS DVVSMRTRAE KRGDRYVLTG SKMWITNGPE AETLVVYAKT
     DPAAGPRGIT AFLIEKGMKG FSTAQKLDKL GMRGSDTCEL VFEECEVPEE NVLGEVGRGV
     NVLMSGLDYE RAVLAAGPLG IMQACLDVVL PYVHERKQFG QPIGEFQLVQ GKLADMYVAT
     NAAKAYVYAV AQACDRGETT REDAAGAILY AAERATQCAL DAIQLLGGNG YINDYPTGRL
     LRDAKLYEIG AGTSEIRRML IGRELFAKSS A
//

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