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3HIDH_DROME
ID   3HIDH_DROME             Reviewed;         324 AA.
AC   Q9V8M5; Q0E926; Q86R98; Q9V8M6;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE            Short=HIBADH;
DE            EC=1.1.1.31;
DE   Flags: Precursor;
GN   ORFNames=CG15093;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC         oxopropanoate + H(+) + NADH; Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC         ChEBI:CHEBI:57945; EC=1.1.1.31;
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC       dehydrogenase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL39202.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE013599; AAF57639.2; -; Genomic_DNA.
DR   EMBL; AY069057; AAL39202.2; ALT_INIT; mRNA.
DR   RefSeq; NP_001188972.1; NM_001202043.2.
DR   RefSeq; NP_611373.1; NM_137529.4.
DR   RefSeq; NP_725824.1; NM_166306.3.
DR   AlphaFoldDB; Q9V8M5; -.
DR   SMR; Q9V8M5; -.
DR   BioGRID; 62836; 1.
DR   DIP; DIP-22109N; -.
DR   IntAct; Q9V8M5; 1.
DR   STRING; 7227.FBpp0085821; -.
DR   PaxDb; Q9V8M5; -.
DR   PeptideAtlas; Q9V8M5; -.
DR   PRIDE; Q9V8M5; -.
DR   DNASU; 37166; -.
DR   EnsemblMetazoa; FBtr0086639; FBpp0085821; FBgn0034390.
DR   EnsemblMetazoa; FBtr0086640; FBpp0085822; FBgn0034390.
DR   EnsemblMetazoa; FBtr0303846; FBpp0292854; FBgn0034390.
DR   GeneID; 37166; -.
DR   KEGG; dme:Dmel_CG15093; -.
DR   UCSC; CG15093-RA; d. melanogaster.
DR   FlyBase; FBgn0034390; CG15093.
DR   VEuPathDB; VectorBase:FBgn0034390; -.
DR   eggNOG; KOG0409; Eukaryota.
DR   GeneTree; ENSGT00940000173744; -.
DR   HOGENOM; CLU_035117_6_0_1; -.
DR   InParanoid; Q9V8M5; -.
DR   OMA; WSSEVNN; -.
DR   OrthoDB; 812358at2759; -.
DR   PhylomeDB; Q9V8M5; -.
DR   Reactome; R-DME-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00362; -.
DR   BioGRID-ORCS; 37166; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; CG15093; fly.
DR   GenomeRNAi; 37166; -.
DR   PRO; PR:Q9V8M5; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0034390; Expressed in adult Malpighian tubule (Drosophila) and 24 other tissues.
DR   ExpressionAtlas; Q9V8M5; baseline and differential.
DR   Genevisible; Q9V8M5; DM.
DR   GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR   GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; ISS:FlyBase.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0006574; P:valine catabolic process; ISS:FlyBase.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR011548; HIBADH.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029154; NADP-bd.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01692; HIBADH; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   2: Evidence at transcript level;
KW   Branched-chain amino acid catabolism; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..324
FT                   /note="Probable 3-hydroxyisobutyrate dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000007161"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000250"
FT   BINDING         29..58
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..93
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  33883 MW;  A39B534753EAE83E CRC64;
     MSLRVMSPAM LNAWSQTLVR AMSTQGGAKN IGFVGLGNMG ANMASNLIKA GHKLHVFDIS
     KPACDGLAAK GATVYAKTSE LAKNSDFVIT MLPNNAIVDA SYDEMTADGV NKDTIFIDSS
     TISPDLVKSL QKKISAKGAR FIDAPVSGGV PGAEQATLTF MVGGTEAEYN AVKAVLECMG
     KKITHCGVYG MGQAAKLCNN MMLAISMIGV SEAMNLAVRQ GLDANVFAEI INSSTGRCWA
     SEIYNPVPGV CPSAPANRDY AGGFSSALIT KDLGLASGVA NASNSPIPLG SLAHKVYQSL
     CDKGLGNKDF SVVYDLMKKE KFSV
 
 
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