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D2HDH_ORYSJ
ID   D2HDH_ORYSJ             Reviewed;         559 AA.
AC   Q7XI14; B9FVX0;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable D-2-hydroxyglutarate dehydrogenase, mitochondrial;
DE            EC=1.1.99.39;
DE   Flags: Precursor;
GN   Name=D2HGDH; OrderedLocusNames=Os07g0187200, LOC_Os07g08950;
GN   ORFNames=OsJ_23376, OSJNBb0084L07.2, P0506C07.26;
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=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   [2]
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   [3]
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).
CC   -!- FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-
CC       ketoglutarate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC         Xref=Rhea:RHEA:38295, ChEBI:CHEBI:13193, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.39;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per monomer. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEE66707.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP004384; BAC79943.1; -; Genomic_DNA.
DR   EMBL; AP005179; BAD31069.1; -; Genomic_DNA.
DR   EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000144; EEE66707.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015646834.1; XM_015791348.1.
DR   RefSeq; XP_015646835.1; XM_015791349.1.
DR   AlphaFoldDB; Q7XI14; -.
DR   SMR; Q7XI14; -.
DR   STRING; 4530.OS07T0187200-01; -.
DR   PaxDb; Q7XI14; -.
DR   PRIDE; Q7XI14; -.
DR   GeneID; 4342598; -.
DR   KEGG; osa:4342598; -.
DR   eggNOG; KOG1232; Eukaryota.
DR   InParanoid; Q7XI14; -.
DR   OrthoDB; 515900at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051990; F:(R)-2-hydroxyglutarate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
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; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..80
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           81..559
FT                   /note="Probable D-2-hydroxyglutarate dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000393390"
FT   DOMAIN          131..310
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   559 AA;  61097 MW;  F4BDDA06DA0F0EF3 CRC64;
     MARRAAAGLL RRHLGPLAAG ETLQARGMYP KQYGAANHAF SRFYSIQGQQ RSLYGFRTNV
     ETDDTQQSAR MNFEVQKRSF SSAAAHVQRN PAYSVLNSDD VSYFKSILGD SGVVQDEDRV
     SVANMDWMGK YKGSSQLLLL PKSTAEVSKI LSYCNSRRLA VVPQGGNTGL VGGSVPVYDE
     VIISLGGMDK IITFDNVNGI LTCEAGCVLE NLSSYVENKG FIMPLDLGAK GSCHIGGNIS
     TNAGGLRFIR YGSLHGSVLG LEVVLADGTV LDMLTTLRKD NTGYDLKHLF IGSEGSLGIV
     TKIAILTPAK LPSTNVAFLS CNDYISCQKL LLAARRSLGE ILSAFEFMDR HCINLAMKYL
     EGVHNPLPVS PFNFYVLIET TGSDESYDKA KLEAFLLRSM EDGLVADGVI AQDISQASNF
     WRIREGISEA SVKVGAVYKY DLSIPVEKLY DIVEEMRSRV GDMGQVLGYG HLGDGNLHLN
     ILSTKYSDKM LAQIEPFVYE WTSKQRGSIS AEHGLGLMKA EKIHYSKSSE AVQLMASIKK
     LLDPNSILNP YKVLPQSVL
 
 
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