ID F6HLP5_VITVI Unreviewed; 609 AA.
AC F6HLP5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN OrderedLocusNames=VIT_08s0007g05710 {ECO:0000313|EMBL:CCB55301.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB55301.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005147}.
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DR EMBL; FN595991; CCB55301.1; -; Genomic_DNA.
DR RefSeq; XP_002274214.2; XM_002274178.4.
DR AlphaFoldDB; F6HLP5; -.
DR STRING; 29760.F6HLP5; -.
DR PaxDb; 29760-VIT_08s0007g05710-t01; -.
DR EnsemblPlants; Vitvi08g01676_t001; Vitvi08g01676_P001; Vitvi08g01676.
DR Gramene; Vitvi08g01676_t001; Vitvi08g01676_P001; Vitvi08g01676.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_021072_0_0_1; -.
DR InParanoid; F6HLP5; -.
DR OrthoDB; 1048at2759; -.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000009183; Chromosome 8.
DR ExpressionAtlas; F6HLP5; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016633; F:galactonolactone dehydrogenase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_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; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR010029; GL_DH.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR NCBIfam; TIGR01676; GLDHase; 1.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 2.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT DOMAIN 117..288
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 18..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 69176 MW; 6226014F5FEA2FC5 CRC64;
MLRALSLRRS LRAFHHYHHH HHQPTNPHSN LLKALSSTTS PNPNPNLTRP FSSLSSSPSS
EAEFRKYLGY FALLLGCGIA TYYSFPFSDS AKHKKAQLFR YAPLPDDLHT VSNWSGTHEV
QTRVFHQPES LEELEQIVKE ANEKKQKIRP VGSGLSPNGI GLTRAGMVNL ALMDNVLDVD
VEKKRVRVQA GIRVQQLVDA IKDYGITLQN FASIREQQIG GIVQVGAHGT GARLPPIDEQ
VISMKLVTPA KGTIEVSKER DPELFYLARC GLGGLGVVAE VTLQCVERQE LVEHTVVSNM
KEIKKNHKKL LSENKHVKYL YIPYTDTVVV VTCNPVSKWK GPPKFKPKYS RDEAIQHVRD
LYQESLKKYS PEAITAKSSD NSEPDINELS FTELRDKLLA LDPLNKDHVI QVNQAEAEFW
RKSEGYRVGW SDEILGFDCG GQQWVSETCF PAGTLAKPSM KDLEYIEDLK KLIEKEEIPA
PAPIEQRWTQ SSKSPMSPAS SSAEDDIFSW VGIIMYLPTM DARQRKEITE EFFHYRRLSQ
TQLWDLYSAY EHWAKIEVPK DKDELAALQA RLRKRFPVDE YNKARKELDP NRILSNNMLG
KLFPSSDTI
//
