ID Q9I1D2_PSEAE Unreviewed; 411 AA.
AC Q9I1D2;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=SfnB family sulfur acquisition oxidoreductase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=PA2346 {ECO:0000313|EMBL:AAG05734.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG05734.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG05734.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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DR EMBL; AE004091; AAG05734.1; -; Genomic_DNA.
DR PIR; C83351; C83351.
DR RefSeq; NP_251036.1; NC_002516.2.
DR RefSeq; WP_003106870.1; NZ_QZGE01000021.1.
DR AlphaFoldDB; Q9I1D2; -.
DR SMR; Q9I1D2; -.
DR STRING; 208964.PA2346; -.
DR PaxDb; 208964-PA2346; -.
DR GeneID; 879885; -.
DR KEGG; pae:PA2346; -.
DR PATRIC; fig|208964.12.peg.2455; -.
DR PseudoCAP; PA2346; -.
DR HOGENOM; CLU_018204_10_0_6; -.
DR InParanoid; Q9I1D2; -.
DR OrthoDB; 6502068at2; -.
DR PhylomeDB; Q9I1D2; -.
DR BioCyc; PAER208964:G1FZ6-2385-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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; 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; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000002438}.
FT DOMAIN 43..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 149..226
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 253..386
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 411 AA; 44925 MW; 4F16F819B089FD55 CRC64;
MTDETAPKDL RDQAPRLLPA RLIENDAQAL QAAHEVAGLA RREAALRDRE RRLPWQELEL
FTRLGLGGIG IPRAHGGAQV SHVTLAEVFR VICAADPALG QIPQNQFGLL SVIDNVASPA
QKRKLFRGIL DGRRLANAGP ERNTRHTLEL KARVRRDGDG YRVSGEKFYS TGALFAHWVA
VKAIDEEERA VMLFVERGAP GLRIVDDWSG FGQRTTASGT VLLDEVPVAG DMLIHNGLLA
EIPSLQGAVS QLIQAAIDAG IAQAALDDAQ AFVRERSRPW IDAQVERASD ELYSIAEVGR
LQIELHAANA LLEKAGQVLD EVAARPVDAE SAARASIAVA EAKVLSTEIS LAASEKLFEL
AGSRATLAEF NLDRHWRNAR THTLHDPVRW KVHAVGDYYL NGARPARHSW I
//
