GLDH1_ORYSJ
ID GLDH1_ORYSJ Reviewed; 583 AA.
AC Q2RAP0; A0A0P0XYT6; Q0IUP6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=L-galactono-1,4-lactone dehydrogenase 1, mitochondrial;
DE EC=1.3.2.3;
DE Flags: Precursor;
GN Name=GLDH1; OrderedLocusNames=Os11g0143500, LOC_Os11g04740;
GN ORFNames=OsJ_32931;
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;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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=BAF27569.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DP000010; ABA91419.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF27569.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014967; BAT12639.1; -; Genomic_DNA.
DR EMBL; CM000148; EAZ17409.1; -; Genomic_DNA.
DR EMBL; AK102697; BAG95677.1; -; mRNA.
DR RefSeq; XP_015616655.1; XM_015761169.1.
DR AlphaFoldDB; Q2RAP0; -.
DR SMR; Q2RAP0; -.
DR STRING; 4530.OS11T0143500-01; -.
DR PaxDb; Q2RAP0; -.
DR PRIDE; Q2RAP0; -.
DR EnsemblPlants; Os11t0143500-01; Os11t0143500-01; Os11g0143500.
DR GeneID; 4349749; -.
DR Gramene; Os11t0143500-01; Os11t0143500-01; Os11g0143500.
DR KEGG; osa:4349749; -.
DR eggNOG; KOG4730; Eukaryota.
DR HOGENOM; CLU_021072_0_0_1; -.
DR InParanoid; Q2RAP0; -.
DR OMA; WDEYSAY; -.
DR OrthoDB; 1134169at2759; -.
DR BRENDA; 1.3.2.3; 8948.
DR PlantReactome; R-OSA-1119410; Ascorbate biosynthesis.
DR UniPathway; UPA00132; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR Genevisible; Q2RAP0; 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_0000372085"
FT CHAIN 79..583
FT /note="L-galactono-1,4-lactone dehydrogenase 1,
FT mitochondrial"
FT /id="PRO_0000372086"
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"
SQ SEQUENCE 583 AA; 65586 MW; 60F4A30CBD072627 CRC64;
MRRLLLAGIL RRASSSPSSH HHLHLVRALS ASSPLPASDA DLRKYAGYAL LLLGCGAATY
YSFPLPPDAL HKKAVPFKYA PLPDDLHAVS NWSATHEVHT RVLLQPDSLP ALHDALAAAH
GECRKLRPLG SGLSPNGLAL SRAGMVNLAL MDKVLGVDAK KKTVTVQAGI RVAELVDALR
EHGLTLQNFA SIREQQVGGI IQVGAHGTGA RLPPIDEQVI SMKLVTPAKG TIELSREKDP
DLFYLARCGL GGLGVVAEVT LQCVERHQLI EHTFVSNADE VKKNHKKWLS ENKHIKYLWI
PYTDTVVVVQ CNPPSRWRTP KFTSKYGKDE AIQHVRDLYH ESLKKYRTKA ESNDPEVDQL
SFTELRDRLL TLDPLDKDHV IRINKAEAEY WKKSEGYRMG WSDEILGFDC GGQQWVSETC
FPAGTLAKPN MKDLDYIEEL LQLIEKEDIP APAPIEQRWT ACSRSPMSPA SSSQEDDIFS
WVGIIMYLPT SDARQRKEIT EEFFNYRSKT QTNLWDGYSA YEHWAKIEVP KDKDELAELQ
ARLRKRFPVD AYNKARMELD PNKVLSNAKL EKLFPVTEVQ HEK
