PANB2_ORYSJ
ID PANB2_ORYSJ Reviewed; 399 AA.
AC Q9AWZ7; A0A0P0UZU4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase 2, mitochondrial;
DE EC=2.1.2.11;
DE AltName: Full=Ketopantoate hydroxymethyltransferase 2;
DE Flags: Precursor;
GN Name=KPHMT2; Synonyms=PANB2;
GN OrderedLocusNames=Os01g0225500, LOC_Os01g12570;
GN ORFNames=P0443E07.7, P0492F05.16;
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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).
CC -!- FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl
CC group from 5,10-methylenetetrahydrofolate is transferred onto alpha-
CC ketoisovalerate to form ketopantoate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-
CC oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-
CC dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57453; EC=2.1.2.11;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP002900; BAB92104.1; -; Genomic_DNA.
DR EMBL; AP002902; BAB32713.1; -; Genomic_DNA.
DR EMBL; AP008207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014957; BAS71111.1; -; Genomic_DNA.
DR RefSeq; XP_015645815.1; XM_015790329.1.
DR AlphaFoldDB; Q9AWZ7; -.
DR SMR; Q9AWZ7; -.
DR STRING; 4530.OS01T0225500-00; -.
DR PaxDb; Q9AWZ7; -.
DR PRIDE; Q9AWZ7; -.
DR EnsemblPlants; Os01t0225500-00; Os01t0225500-00; Os01g0225500.
DR GeneID; 107275880; -.
DR Gramene; Os01t0225500-00; Os01t0225500-00; Os01g0225500.
DR KEGG; osa:107275880; -.
DR eggNOG; KOG2949; Eukaryota.
DR HOGENOM; CLU_036645_2_1_1; -.
DR InParanoid; Q9AWZ7; -.
DR OMA; TEDMIGA; -.
DR OrthoDB; 1439584at2759; -.
DR PlantReactome; R-OSA-1119496; Pantothenate biosynthesis I.
DR PlantReactome; R-OSA-1119544; Pantothenate biosynthesis II.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q9AWZ7; OS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
DR CDD; cd06557; KPHMT-like; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR HAMAP; MF_00156; PanB; 1.
DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR20881; PTHR20881; 1.
DR Pfam; PF02548; Pantoate_transf; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR00222; panB; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Mitochondrion; Pantothenate biosynthesis;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..90
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 91..399
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase 2,
FT mitochondrial"
FT /id="PRO_0000429569"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 125..126
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 41233 MW; BD28EAD9C97F75CD CRC64;
MSFSRLLTPR ILLDTTAVFP PSSSVVAPSL SRQLRCTRTG GSPPAPPHRL VARRAMSNGA
AEPAIYGGGG GAQQAASSAA ARRVTLATLR GKHRRGEPIS MVTAYDYPSG VHVDAAGFDI
CLVGDSAAMV AHGHDNTLPI SLDLMIEHCR AVARGAARTF LVGDLPFGSY EASTAQAVGS
AVRVMKEGGV NSIKLEGSAP SRISAARAIV DAGIAVMGHI GLTPQSVSAL GGFRPQGKTV
ESAVKVVEAA LALQEAGCFA VVLECVPAPV AAAATSALTI PTIGIGAGPF CSGQVLVYHD
LLGTFQTSHA KVSPKFCKQY GNIGDVINRA LSKYKQEVET QSFPGPSHTP YKLAATDVDA
FLNALKMKGL NVAADAAADA VEYTDEKEIN GTPQLKVYA
