GLDH2_ORYSJ
ID GLDH2_ORYSJ Reviewed; 583 AA.
AC Q2QXY1; A0A0P0Y6V7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=L-galactono-1,4-lactone dehydrogenase 2, mitochondrial;
DE EC=1.3.2.3;
DE Flags: Precursor;
GN Name=GLDH2; OrderedLocusNames=Os12g0139600, LOC_Os12g04520;
GN ORFNames=OsJ_35179;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of ascorbic acid. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(III)-[cytochrome c] + L-galactono-1,4-lactone = 4 Fe(II)-
CC [cytochrome c] + 5 H(+) + L-dehydroascorbate; Xref=Rhea:RHEA:32367,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17464, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:58539; EC=1.3.2.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF29139.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA96408.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF29139.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014968; BAT15829.1; -; Genomic_DNA.
DR EMBL; CM000149; EAZ19601.1; -; Genomic_DNA.
DR EMBL; AK241565; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015619621.1; XM_015764135.1.
DR AlphaFoldDB; Q2QXY1; -.
DR SMR; Q2QXY1; -.
DR STRING; 4530.OS12T0139600-01; -.
DR PaxDb; Q2QXY1; -.
DR PRIDE; Q2QXY1; -.
DR EnsemblPlants; Os12t0139600-01; Os12t0139600-01; Os12g0139600.
DR GeneID; 4351464; -.
DR Gramene; Os12t0139600-01; Os12t0139600-01; Os12g0139600.
DR KEGG; osa:4351464; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_021072_0_0_1; -.
DR InParanoid; Q2QXY1; -.
DR OMA; DPLNKNH; -.
DR OrthoDB; 1134169at2759; -.
DR BRENDA; 1.3.2.3; 8948.
DR PlantReactome; R-OSA-1119410; Ascorbate biosynthesis.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QXY1; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-EC.
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; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 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.
DR InterPro; IPR010029; GL_DH.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR43762; PTHR43762; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR TIGRFAMs; TIGR01676; GLDHase; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT PROPEP 37..78
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000372087"
FT CHAIN 79..583
FT /note="L-galactono-1,4-lactone dehydrogenase 2,
FT mitochondrial"
FT /id="PRO_0000372088"
FT TRANSMEM 45..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 95..266
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CONFLICT 193
FT /note="R -> Q (in Ref. 6; AK241565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 65702 MW; F2952A474EE67582 CRC64;
MRRLLLAGIL RRASSSPSSH HHLHLVRALS ASSPLPASDA DLRKYAGYAL LLLGCGAATY
YSFPLPPDAL HKKAVPFKYA PLPDDLHAVS NWSATHEVHT RVLLQPDSLP VLHDALAAAH
GERRKLRPLG SGLSPNGLAL SRAGMVNLAL MDKVLDVDAK KKTVTVQAGI RVAELVDTLR
EHGLTLQNFA SIREQQVGGI IQVGAHGTGA RLPPIDEQVI SMKLVTPAKG TIELSREKDP
DLFYLARCGL GGLGVVAEVT LQCVERHQLI EHTFVSSADE VKKNHKKWLS ENKHIKYLWI
PYTDTVVVVQ CNPPSRWRTP KFTSKYGKDE AIQHVRDLYR ESLKKYRTKA ESNDPEVDQL
SFTELRDRLL ALDPLDKDHV IRINKAEAEY WKKSEGYRMG WSDEILGFDC GGQQWVSETC
FPAGTLAKPN MKDLDYIEEL LQLIEKEDIP APAPIEQRWT ACSRSPMSPA SSSQEDDIFS
WVGIIMYLPT SDARQRKEIT EEFFNYRSKT QTNLWDGYSA YEHWAKIEVP KDKDELTELL
ARLRKRFPVD AYNKARMELD PNKVLSNAKL EKLFPVTEVQ HVK
