GenomeNet

Database: UniProt
Entry: A0A0L9URZ2_PHAAN
LinkDB: A0A0L9URZ2_PHAAN
Original site: A0A0L9URZ2_PHAAN 
ID   A0A0L9URZ2_PHAAN        Unreviewed;       808 AA.
AC   A0A0L9URZ2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125};
DE            EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125};
GN   ORFNames=LR48_Vigan06g067300 {ECO:0000313|EMBL:KOM45367.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
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; Vigna.
OX   NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM45367.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA   Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA   Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA   Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT   high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC   -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC       oxidation pathway of lipid degradation.
CC       {ECO:0000256|ARBA:ARBA00003842}.
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   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM003376; KOM45367.1; -; Genomic_DNA.
DR   RefSeq; XP_017426124.1; XM_017570635.1.
DR   AlphaFoldDB; A0A0L9URZ2; -.
DR   STRING; 3914.A0A0L9URZ2; -.
DR   EnsemblPlants; KOM45367; KOM45367; LR48_Vigan06g067300.
DR   GeneID; 108334714; -.
DR   Gramene; KOM45367; KOM45367; LR48_Vigan06g067300.
DR   KEGG; var:108334714; -.
DR   OMA; ASEVWPE; -.
DR   OrthoDB; 601859at2759; -.
DR   Proteomes; UP000053144; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 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|PIRSR:PIRSR028937-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          344..564
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          664..793
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        739
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT   BINDING         297..312
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ   SEQUENCE   808 AA;  88434 MW;  1F4BF333E5309B74 CRC64;
     MEDRTIGRSG SSRKGSFRFG IGVDGKKDHT VVELGSIDTH RLLLSGGERQ KKQQPLTNSL
     SSRQMKSLSA LCDSILPSVD HSVHTSDESV NKFYRISASM AGTPELLGGV MCEKLKHPLT
     GLLKLALWGL STWFGTLILC GMGCVSTKFP FIHSFPELSL QKRQDIMRSW SLSYIRLLRL
     LFRTIKLLTL LVFFTQTDES EENLSWKAIG YCGPDPKFKA QLKNHFLDGK SKEAEDDKED
     EDAEEVIGPL YKGLVHLNNP RDIAADALRR LGFSVSVVRR KHKAAANLSS PSLVIQCDAV
     VVGSGSGGGV IAGVLAKAGY KVLVLEKGGY SARNNLSLLE GQSMDQMYLN AGLVASDDMG
     MFILSGSTVG GGSAVNWSAS IKTPQHVCKE WCEKHGLELF ESELYREALD AVCEKMGVQS
     EIEDEGFNNA VLRKGCQEMG YPVNTIPRNS SSDHYCGWCC MGCKDGKKKG TLETWLVDLV
     KSGNGAILPG CEALKVLHKN MEGRDRKVAG GVAFEFEYKG IKDICVVESK VTIVACGALC
     TPALLKRSGL RNQNIGRNLH LHPVTMAWGY FPDEPASEVW PEANKKSYEG GIMTAMSSVV
     AEFEQSGYGA VIQTPSLHPG MFSIVTPWTS GVDIRDRMRK FSRTAHVFAL ARDKGSGTVE
     SPHRISYKLA GVDEKNLQKG IDKVLRILAA AGAEEIGTHH NKGRTLNVKQ VSYHEFEKFV
     KEESSRPLTD LSTPLCSAHQ MGSCRMGSNP KQSVVNQTGE TWEMEGLYVA DTSVFPTALG
     VNPMVTVQAI AYCVAQSVLE VLRRKRSK
//
DBGET integrated database retrieval system