ID A0A0D2RLW2_GOSRA Unreviewed; 491 AA.
AC A0A0D2RLW2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=monodehydroascorbate reductase (NADH) {ECO:0000256|ARBA:ARBA00038920};
DE EC=1.6.5.4 {ECO:0000256|ARBA:ARBA00038920};
GN ORFNames=B456_008G250000 {ECO:0000313|EMBL:KJB52193.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB52193.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB52193.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-
CC ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:59513; EC=1.6.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036831};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; CM001747; KJB52193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2RLW2; -.
DR EnsemblPlants; KJB52193; KJB52193; B456_008G250000.
DR Gramene; KJB52193; KJB52193; B456_008G250000.
DR Proteomes; UP000032304; Chromosome 8.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR048618; MDHAR3-like_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF6; MONODEHYDROASCORBATE REDUCTASE, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR Pfam; PF21791; MDHAR3-like_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT DOMAIN 59..369
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 388..471
FT /note="Monodehydroascorbate reductase 3-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21791"
SQ SEQUENCE 491 AA; 53425 MW; DF87691AE78481B6 CRC64;
MYPARKAMAS LSNSLQLKHG LTSWCPGSSS LTRRLPSSSI RFRSFVVAAS SFSNDNREFV
IVGGGNAAGY AARTFVEHGM ADGKLCIVSK EAYAPYERPA LTKGYLFPLD KKPARLPGFH
TCVGSGGERQ TPEWYKEKGI EMIYEDPVTA IDTEKQTLTT NSGKLLKYGS LIIATGCTAS
RFPDKIGGNL PGVHYIRDVA DANSLISSLA QKVVIVGGGY IGMEVAAAAV AWKLDTSIIF
PENQLLQRLF TPSLAQRYEE LYKEYGVKFL KGASIKNLEA GPDGRVAAVK LGDGSTVEAD
MVVIGIGAKP AVSPFEVVGL NNTVGGIQVD GLFRTSVPGI FAVGDVAAFP LKMYDRVARV
EHVDHARRSA QHCVKSLLSA QTHTYDYLPY FYSRVFEYEG SPRKVWWQFF GDNVGETVEI
GNFDPKIATF WIDSGKLKGV LLESGNAEEF KLLPELARNQ PSIDKAKLEK ASLVEEALEI
AKASLQVVQK A
//
