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Database: UniProt
Entry: Q0VPP1_ALCBS
LinkDB: Q0VPP1_ALCBS
Original site: Q0VPP1_ALCBS 
ID   Q0VPP1_ALCBS            Unreviewed;       543 AA.
AC   Q0VPP1;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   SubName: Full=Alkylglycerone-phosphate synthase {ECO:0000313|EMBL:CAL16857.1};
DE            EC=2.5.1.26 {ECO:0000313|EMBL:CAL16857.1};
GN   OrderedLocusNames=ABO_1409 {ECO:0000313|EMBL:CAL16857.1};
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595 {ECO:0000313|EMBL:CAL16857.1, ECO:0000313|Proteomes:UP000008871};
RN   [1] {ECO:0000313|EMBL:CAL16857.1, ECO:0000313|Proteomes:UP000008871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2
RC   {ECO:0000313|Proteomes:UP000008871};
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR   EMBL; AM286690; CAL16857.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0VPP1; -.
DR   STRING; 393595.ABO_1409; -.
DR   KEGG; abo:ABO_1409; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_2_0_6; -.
DR   OMA; GTISHQH; -.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:UniProtKB-EC.
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:UP000008871};
KW   Transferase {ECO:0000313|EMBL:CAL16857.1}.
FT   DOMAIN          91..271
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        454
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         123..129
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         255..261
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            306
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   543 AA;  60152 MW;  215C0AD6D44830EE CRC64;
     MKIRSACMRR WNGWGDSNNH YPLKPSGLAF VQQRLGRAEP LPDAEMTAVV AKVPASRLPE
     HPSVDTRPET RLRHARGQSL PDWLAMRSGE FERFPDGVAT PASSGAVREL LDWALEQGIT
     VIPYGGGTSV AGHINPPESD APVLTLSLAG MDQLMDLDTE SQIATFGAGT PGPMVEQQLR
     ERGYMLGHFP QSWELSTIGG WVASRSSGQQ SMRYGRIEQM FAGGRVETPK GTLIIPTMPA
     SSAGPDLREI ILGSEGRMGV ITEVKVRVTP LPETESFQVA FAPDWETGKE LVRKMIQAKI
     PLSMLRLSNA EETRTHLMLA GHEKLVGILH RYLGVRGCGD SKCMITFGVT GDKSQARYVL
     SQTRKHIRQA GGVMVGRLLG KKWEESRFRS PYLRHGLWEH GYVVDTFETA VDWNRVTSAV
     ETMEKAVRDN AGDGEQVHVF THLSHLYSQG SSIYTTYVFR CSDSYEKTLA RWRVLKEAAS
     NAIVASGGTI SHQHGVGRDH ARWLHHEKGE LGMAVLDRLV NHFDPQHRLN PGCLIENAPR
     TIR
//
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