ID A0A0N0E1M9_9PSED Unreviewed; 400 AA.
AC A0A0N0E1M9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Sulfur acquisition oxidoreductase, SfnB family {ECO:0000313|EMBL:KPA87877.1};
GN ORFNames=PF66_05454 {ECO:0000313|EMBL:KPA87877.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA87877.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA87877.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA87877.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
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:KPA87877.1}.
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DR EMBL; JSYZ01000025; KPA87877.1; -; Genomic_DNA.
DR RefSeq; WP_054064319.1; NZ_JSYZ01000025.1.
DR AlphaFoldDB; A0A0N0E1M9; -.
DR STRING; 50340.PF66_05454; -.
DR PATRIC; fig|50340.43.peg.3166; -.
DR OrthoDB; 6502068at2; -.
DR Proteomes; UP000037931; 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 InterPro; IPR023922; S04_starv_induced_SfnB.
DR NCBIfam; TIGR04022; sulfur_SfnB; 1.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
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 19..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 244..375
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 400 AA; 43341 MW; 2DC1306B1E9D3C6A CRC64;
MTAAAKPTTV AYVIRSDEEA IAAARQLAAR FAVEASARDR ERRLPGAELD EFSATGLWAI
TVPKAYGGAG VSYVTVAEVI KIISAADPSL GQIPQNHLGV LDILLQTASE EQKRHYFAKV
LEGYRFGNAF SEAKSRNAGT FDTRIRFDGD SAVINGEKFY CTGALFAHIV PVVGLDEAGN
AQIAFVERHA PGLTIVDNWD GFGQRTTASG NALFVDVRVP RSSVIPAHLA FDQPTANGPI
SQIIQAAVDT GIALGALEET KRHARQARPW IDSQQEHGWQ DPFSLAAIGD LEWRVHGTEA
ILEKAGRAID HALAQPSEDS VAEASVVVAQ AKVLSAETSL LAASKLFELA GTRSVLGKHN
LDRHWRNART HTLHDPARWK YHLIGNYLLN GVKPARHAWN
//
