ID V7BGM7_PHAVU Unreviewed; 741 AA.
AC V7BGM7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
DE EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
GN ORFNames=PHAVU_007G124200g {ECO:0000313|EMBL:ESW16038.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW16038.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
CC -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC oxidation pathway of lipid degradation. {ECO:0000256|ARBA:ARBA00003842,
CC ECO:0000256|PIRNR:PIRNR028937}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain primary fatty alcohol + O2 = a long-chain fatty
CC aldehyde + H2O2; Xref=Rhea:RHEA:22756, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17176, ChEBI:CHEBI:77396; EC=1.1.3.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000920,
CC ECO:0000256|PIRNR:PIRNR028937};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|PIRNR:PIRNR028937}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|PIRNR:PIRNR028937}.
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DR EMBL; CM002294; ESW16038.1; -; Genomic_DNA.
DR RefSeq; XP_007144044.1; XM_007143982.1.
DR AlphaFoldDB; V7BGM7; -.
DR STRING; 3885.V7BGM7; -.
DR EnsemblPlants; ESW16038; ESW16038; PHAVU_007G124200g.
DR GeneID; 18625677; -.
DR Gramene; ESW16038; ESW16038; PHAVU_007G124200g.
DR KEGG; pvu:PHAVU_007G124200g; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR OMA; NTGVNPQ; -.
DR OrthoDB; 601859at2759; -.
DR PhylomeDB; V7BGM7; -.
DR Proteomes; UP000000226; Chromosome 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR012400; Long_Oxdase.
DR PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF10; LONG-CHAIN-ALCOHOL OXIDASE FAO3; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF028937; Lg_Ch_AO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR028937-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR028937};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR028937};
KW Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 236..269
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 283..503
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 596..728
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 675
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT BINDING 235..250
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ SEQUENCE 741 AA; 81452 MW; 67826659C4613BB6 CRC64;
MKRECHPVLR GGRRGSRNTT DPLPSAEMES LTSICEAFFP PLQLEHLDKH NSKTKAVQHF
WKSSASQFPI PQETADMLIK RALKEALIFV RLILWMLSTR LGTLLLCGTL CLSKKWPCIH
NFSNISLDNR EKVLQKWFKH RFFTPIRLAF LYVKVLCLFV FFSQCDEKGQ NPAWEAVGYK
VDTDGITKQV QKERPLEKGI VEGRNESDWS LPKSLGEKGL EVSVDAGNNV LGIKCDVVIV
GSGCGGGVAA ATLASSGLKV LVLEKGNYYT SSDYSSLEGP SLNELYELGG TFASWDGNMA
ILAGSTVGGG SAVNWAASIR TPDSVLKEWE KEHKLSLFSS HEYLSAMDMV CKRIGVTDKC
VEEGLQNQVL RKGCKNLGLQ VDYVPRNSSE RHYCGSCNYG CTRGDKQGTE VTWLVDAVDH
DAVILTGTKA ERFILGNNKG GRVRKKKCLG VMANVLTNNI TWRLKVEAKV TVSACGALLT
PPLMISSGLK NKHIGKNLHM HPVLMSWGYF PDSNSDLKGK CYEGGIITSV HKVVSEDSNV
KAIVETPALG PAVLSTLLPW VSGSDFKERM LKYSRTVHLI TIIRDKGCGV VRSEGRVHYD
LDESDKENIR DGVKQALRIL IAAGAVEVGT HRSDGQRIEC NGNNEKELER FVESIYATGG
SMSQEEKWSI YSSAHQMGSC KMGMSEKEGA VDENGMSWEA EGLFVCDASL LPTAIGVNPM
ITIQSTAYCV AKRIAAFLGI Q
//
