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
//