ID A0A0Q7YSU1_9SPHN Unreviewed; 415 AA.
AC A0A0Q7YSU1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQZ64547.1};
GN ORFNames=ASD67_08775 {ECO:0000313|EMBL:KQZ64547.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ64547.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ64547.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ64547.1,
RC ECO:0000313|Proteomes:UP000051141};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQZ64547.1}.
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DR EMBL; LMGF01000003; KQZ64547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7YSU1; -.
DR STRING; 1736474.ASD67_08775; -.
DR Proteomes; UP000051141; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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 Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
FT DOMAIN 45..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 262..392
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 415 AA; 45479 MW; E9F92B0E6B05D163 CRC64;
MEMMMPERLA DRRIPAGDDF LSRDEIDAIT PERLIARMQA LKPLVAERAA AAEKERRPDD
DVWAALRKSG YFYLYVPRRF GGLEYDPDTY ISATLPIAEA CPSTGWTACF AAEHNWLIAQ
MPEATQAEVW GRTPYVVAPS AASPPGIATP VDGGFRLSGR WKWGTVVMHA DWIMLNALEP
VEGGPPVVRM MLLRAEEVTV LDTWRMAGMA ATGSNDILVE DVFIPEAYQF AVQPVRSGRG
NGRAVHGPGL YGSPMLPNLC VTAAIPALGA ARQAVQLCRE RLGQHVKLGS MSTSVEKPAG
QMRLARADLL ARSAERTIRA AARENLLLGE IDEPEQTTER IRLRAEIAIA VQQCVEAVRT
CCEAVGSSVH ALDNPMQRLL RDVQVMQSHI VYDLDVATEL HGRALVGLPP NSLLL
//
