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Database: UniProt
Entry: K1E1M7_9MICO
LinkDB: K1E1M7_9MICO
Original site: K1E1M7_9MICO 
ID   K1E1M7_9MICO            Unreviewed;       421 AA.
AC   K1E1M7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EKA60951.1, ECO:0000313|EMBL:RWU82999.1};
GN   ORFNames=B277_10194 {ECO:0000313|EMBL:EKA60951.1}, CWN80_09320
GN   {ECO:0000313|EMBL:RWU82999.1};
OS   Janibacter hoylei PVAS-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA60951.1, ECO:0000313|Proteomes:UP000004474};
RN   [1] {ECO:0000313|EMBL:RWU82999.1, ECO:0000313|Proteomes:UP000288711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU82999.1,
RC   ECO:0000313|Proteomes:UP000288711};
RX   PubMed=19643890; DOI=10.1099/ijs.0.002527-0;
RA   Shivaji S., Chaturvedi P., Begum Z., Pindi P.K., Manorama R.,
RA   Padmanaban D.A., Shouche Y.S., Pawar S., Vaishampayan P., Dutt C.B.,
RA   Datta G.N., Manchanda R.K., Rao U.R., Bhargava P.M., Narlikar J.V.;
RT   "Janibacter hoylei sp. nov., Bacillus isronensis sp. nov. and Bacillus
RT   aryabhattai sp. nov., isolated from cryotubes used for collecting air from
RT   the upper atmosphere.";
RL   Int. J. Syst. Evol. Microbiol. 59:2977-2986(2009).
RN   [2] {ECO:0000313|EMBL:EKA60951.1, ECO:0000313|Proteomes:UP000004474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA60951.1,
RC   ECO:0000313|Proteomes:UP000004474};
RX   PubMed=23144385; DOI=10.1128/JB.01728-12;
RA   Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L.,
RA   Shouche Y.S.;
RT   "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the
RT   Stratospheric Air.";
RL   J. Bacteriol. 194:6629-6630(2012).
RN   [3] {ECO:0000313|EMBL:RWU82999.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU82999.1};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RL   Submitted (NOV-2017) 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|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:EKA60951.1}.
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DR   EMBL; ALWX01000043; EKA60951.1; -; Genomic_DNA.
DR   EMBL; PIPF01000009; RWU82999.1; -; Genomic_DNA.
DR   RefSeq; WP_007927730.1; NZ_PIPF01000009.1.
DR   AlphaFoldDB; K1E1M7; -.
DR   STRING; 1210046.B277_10194; -.
DR   PATRIC; fig|1210046.3.peg.1954; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 2769798at2; -.
DR   Proteomes; UP000004474; Unassembled WGS sequence.
DR   Proteomes; UP000288711; 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; 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; 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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 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|RuleBase:RU362125}.
FT   DOMAIN          150..245
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          262..413
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          56..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  44880 MW;  E4240DA074EF6D54 CRC64;
     MIDLEVPKKF RPLISQARGM AEEVFWPISR KYDVAEHEYP AELDLVSAVI DGMSDGGAGQ
     GAGASSSTRA KDDGAEEGDV AAVGSGRSSK KGAKENKNGS NLSSVLSILE TCRGDVGLTL
     SIPRQGLGNA AIAAVANDEQ KARYAGKWAA MAITEPDVGS DSGAIRTTAV KDGDEYVLNG
     EKIFVTSGER AELVVVWATL DRSLGKTAIK SFVVRRDNPG LQLVRLEHKL GIRASDTAAF
     VLDNCRVPAE DLLGDPEIKI EGGFGGAMQT FDNTRPLVAS MALGLTRASL DKTTELLKEA
     GIEVDWDRPA NVQSAAAAKL IEMEADYQSA YLLTLRAAWM ADNGKPNSME ASMAKAKAGR
     TCVNVSLACV ELAGATGYAE THLLEKWARD SKILDIFEGT QQIQLLVVAR RILGYSSKEL
     K
//
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