UniProt: A0A099J2I0

Database: UniProt
Entry: A0A099J2I0_9MICO

LinkDB:  A0A099J2I0_9MICO 
Original site:  A0A099J2I0_9MICO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (13)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (1)   
All databases (20)   

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ID   A0A099J2I0_9MICO        Unreviewed;       402 AA.
AC   A0A099J2I0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGJ72516.1};
DE   SubName: Full=Glutaryl-CoA dehydrogenase {ECO:0000313|EMBL:MBB5642926.1};
DE            EC=1.3.8.6 {ECO:0000313|EMBL:MBB5642926.1};
GN   ORFNames=BJ997_003474 {ECO:0000313|EMBL:MBB5642926.1}, GY21_14815
GN   {ECO:0000313|EMBL:KGJ72516.1};
OS   Cryobacterium roopkundense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ72516.1, ECO:0000313|Proteomes:UP000029864};
RN   [1] {ECO:0000313|EMBL:KGJ72516.1, ECO:0000313|Proteomes:UP000029864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RuG17 {ECO:0000313|EMBL:KGJ72516.1,
RC   ECO:0000313|Proteomes:UP000029864};
RA   Sisinthy S.;
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5642926.1, ECO:0000313|Proteomes:UP000561726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5642926.1,
RC   ECO:0000313|Proteomes:UP000561726};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) 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:KGJ72516.1}.
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DR   EMBL; JPXF01000068; KGJ72516.1; -; Genomic_DNA.
DR   EMBL; JACHBQ010000001; MBB5642926.1; -; Genomic_DNA.
DR   RefSeq; WP_035837706.1; NZ_JPXF01000068.1.
DR   AlphaFoldDB; A0A099J2I0; -.
DR   STRING; 1001240.GY21_14815; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000029864; Unassembled WGS sequence.
DR   Proteomes; UP000561726; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004361; F:glutaryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; 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; IPR045008; ACX4-like.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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|RuleBase:RU362125,
KW   ECO:0000313|EMBL:MBB5642926.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029864}.
FT   DOMAIN          24..133
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          139..207
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          250..395
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   402 AA;  43421 MW;  CE3B5D6961331DE4 CRC64;
     MSDTAVNSET AVNMDYYLVD DFLTDEERAI RLKVRAFADA EVLPIINDYW DRAAFPFELV
     PKIARLGIVG GTIEGHGCPG LSRLGAGMVS LEMSRADGSI NTFIGVQSGL TMGTINMLGS
     EEQKQRWLPG LAALDLVGAF GLTEPNHGSD SVALETSARL DGAHYVLNGA KRWIGNASFA
     DVVVIWARDE SDGKVKAFVM EKNADGSFPE GYDATVITGK IGKRAILQPD ITITNLRIPA
     ENKLVDGHSF KDAVRVLNST RGGAAWEALG HATAAYETAV TYARDRVQFG KPIASYQLVQ
     NKLANMLAEL TAMQLICFRL ATLADQGKMT GAMASLAKMH TAQKGRWICQ EARDMLGGNG
     LLLENHVARH LTDMEVVHTY EGTDSIQSLL IGRDITGISA FA
//

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