AOX1B_ORYSJ
ID AOX1B_ORYSJ Reviewed; 335 AA.
AC O82766; Q7XPT1;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ubiquinol oxidase 1b, mitochondrial {ECO:0000305};
DE EC=1.10.3.11 {ECO:0000250|UniProtKB:Q39219};
DE AltName: Full=Alternative oxidase 1b {ECO:0000303|PubMed:22994594};
DE Short=OsAOX1B {ECO:0000303|PubMed:22994594};
DE Flags: Precursor;
GN Name=AOX1B {ECO:0000303|PubMed:22994594};
GN OrderedLocusNames=Os04g0600300 {ECO:0000312|EMBL:BAF15673.1},
GN LOC_Os04g51160 {ECO:0000305};
GN ORFNames=OsJ_16033 {ECO:0000312|EMBL:EAZ31868.1},
GN OSJNBa0083N12.12 {ECO:0000312|EMBL:CAE03472.2};
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=9426242; DOI=10.1016/s0378-1119(97)00502-7;
RA Ito Y., Saisho D., Nakazono M., Tsutsumi N., Hirai A.;
RT "Transcript levels of tandem-arranged alternative oxidase genes in rice are
RT increased by low temperature.";
RL Gene 203:121-129(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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).
RN [8]
RP INDUCTION.
RX PubMed=22994594; DOI=10.1111/pce.12013;
RA Li C.R., Liang D.D., Li J., Duan Y.B., Li H., Yang Y.C., Qin R.Y., Li L.,
RA Wei P.C., Yang J.B.;
RT "Unravelling mitochondrial retrograde regulation in the abiotic stress
RT induction of rice ALTERNATIVE OXIDASE 1 genes.";
RL Plant Cell Environ. 36:775-788(2013).
CC -!- FUNCTION: Catalyzes the cyanide-resistant oxidation of ubiquinol and
CC the reduction of molecular oxygen to water, but does not translocate
CC protons and consequently is not linked to oxidative phosphorylation.
CC May increase respiration when the cytochrome respiratory pathway is
CC restricted, or in response to low temperatures.
CC {ECO:0000250|UniProtKB:Q39219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O;
CC Xref=Rhea:RHEA:30255, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976; EC=1.10.3.11;
CC Evidence={ECO:0000250|UniProtKB:Q39219};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q39219};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q39219};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by drought, cold and salt stresses, heat shock,
CC hydrogen peroxide and methyl viologen. {ECO:0000269|PubMed:22994594}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; AB004813; BAA28771.1; -; Genomic_DNA.
DR EMBL; AB004865; BAA28774.1; -; mRNA.
DR EMBL; AL606683; CAE03472.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15673.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90832.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ31868.1; -; Genomic_DNA.
DR EMBL; AK107376; BAG98037.1; -; mRNA.
DR RefSeq; XP_015633631.1; XM_015778145.1.
DR AlphaFoldDB; O82766; -.
DR SMR; O82766; -.
DR STRING; 4530.OS04T0600300-01; -.
DR PaxDb; O82766; -.
DR PRIDE; O82766; -.
DR EnsemblPlants; Os04t0600300-01; Os04t0600300-01; Os04g0600300.
DR GeneID; 4336875; -.
DR Gramene; Os04t0600300-01; Os04t0600300-01; Os04g0600300.
DR KEGG; osa:4336875; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_0_1_1; -.
DR InParanoid; O82766; -.
DR OMA; WRWNCFR; -.
DR OrthoDB; 943747at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102721; F:ubiquinol:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010230; P:alternative respiration; IBA:GO_Central.
DR CDD; cd01053; AOX; 1.
DR Gene3D; 1.20.1260.140; -; 1.
DR InterPro; IPR002680; AOX.
DR InterPro; IPR038659; AOX_sf.
DR PANTHER; PTHR31803; PTHR31803; 1.
DR Pfam; PF01786; AOX; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..335
FT /note="Ubiquinol oxidase 1b, mitochondrial"
FT /id="PRO_0000440571"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 206
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
SQ SEQUENCE 335 AA; 37251 MW; 7C36F119336B8C12 CRC64;
MSSRMAGATL LRHLGPRLFA AEPVYSGLAA SARGVMPAAA RIFPARMAST SSAGADVKEG
AAEKLPEPAA TAAAAATDPQ NKKAVVSYWG IQPPKLVKED GTEWKWLSFR PWDTYTSDTS
IDVTKHHEPK GLPDKLAYWT VRSLAVPRDL FFQRRHASHA LLLETVAGVP GMVGGMLLHL
RSLRRFEQSG GWIRALLEEA ENERMHLMTF LEVMQPRWWE RALVLAAQGV FFNAYFVGYL
VSPKFAHRFV GYLEEEAVSS YTEYLKDLEA GKIENTPAPA IAIDYWRLPA DATLKDVVTV
IRADEAHHRD LNHFASDIQQ QGMKLKDTPA PIGYH
