ID A0A024HKJ2_PSEKB Unreviewed; 531 AA.
AC A0A024HKJ2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=FAD linked oxidase domain-containing protein {ECO:0000313|EMBL:CDF85139.1};
GN ORFNames=PKB_3801 {ECO:0000313|EMBL:CDF85139.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF85139.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF85139.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF85139.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF85139.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF85139.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR EMBL; HG322950; CDF85139.1; -; Genomic_DNA.
DR RefSeq; WP_043253502.1; NZ_HG322950.1.
DR AlphaFoldDB; A0A024HKJ2; -.
DR STRING; 1301098.PKB_3801; -.
DR KEGG; pkc:PKB_3801; -.
DR PATRIC; fig|1301098.3.peg.3811; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_2_0_6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000025241; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.300.330; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.3450; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR46568; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR PANTHER; PTHR46568:SF1; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR625650-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR625650-
KW 3}; Reference proteome {ECO:0000313|Proteomes:UP000025241}.
FT DOMAIN 84..264
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 448
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 116..122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 248..254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 299
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 531 AA; 58313 MW; 3049FCE0BDCE7C31 CRC64;
MRRWNGWGEE TTAMELPAAG REFLAEAIGP GMALADASLE AVLAKVPASR LAEHPLVIRE
AHDRLMHARG QSLADWLAMR EGEFGLFPDG VAYPQSAEQI RELMRYAEAQ DCLLIPYGGG
TSVAGHINPP ASDKPVLTVS LAHMNRLLEL DEESLVATFG PGANGPQVES QLRARGYTLG
HFPQSWELST LGGWVASRSS GQQSLRYGRI EQLFAGGTLE TFAGSLEIPT FPASSAGPDL
RELVLGSEGR FGVISSVKVR ISRLAEQESF YVVFLPSWER GLAAMRSLAQ ARVQLSMLRL
SNAVETRTQL TLAGHPGQIA WLERYLNWRG AGEDKCMLTF GVTGSRAQNA ASLKAARRML
KDFGGVFTGT LLGRKWEASR FRSPYLRETL WQAGYVVDTL ETATDWSNVD NLLNRIESNL
RGGLAAEGER VHVFTHLSHV YGEGSSIYTT YVFRPASSYA KTHERWRRLK ESTSRVIVEN
RGTISHQHGV GKDHAPYLPT EKGELGMATL RTLAAHFDPA GRLNPGTLLQ D
//
