PANB1_ARATH
ID PANB1_ARATH Reviewed; 347 AA.
AC O82357;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase 1, mitochondrial;
DE EC=2.1.2.11;
DE AltName: Full=Ketopantoate hydroxymethyltransferase 1;
DE Flags: Precursor;
GN Name=KPHMT1; Synonyms=PANB1; OrderedLocusNames=At2g46110;
GN ORFNames=T3F17.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=14675432; DOI=10.1046/j.1365-313x.2003.01940.x;
RA Ottenhof H.H., Ashurst J.L., Whitney H.M., Saldanha S.A., Schmitzberger F.,
RA Gweon H.S., Blundell T.L., Abell C., Smith A.G.;
RT "Organisation of the pantothenate (vitamin B5) biosynthesis pathway in
RT higher plants.";
RL Plant J. 37:61-72(2004).
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:0000269|PubMed:14675432}.
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 Evidence={ECO:0000269|PubMed:14675432};
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:0000269|PubMed:14675432}.
CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000305}.
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DR EMBL; AC005397; AAC62893.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10645.1; -; Genomic_DNA.
DR EMBL; BT004820; AAO44086.1; -; mRNA.
DR EMBL; AK227849; BAE99826.1; -; mRNA.
DR PIR; H84898; H84898.
DR RefSeq; NP_182135.1; NM_130174.5.
DR AlphaFoldDB; O82357; -.
DR SMR; O82357; -.
DR BioGRID; 4554; 3.
DR STRING; 3702.AT2G46110.1; -.
DR MetOSite; O82357; -.
DR PaxDb; O82357; -.
DR PRIDE; O82357; -.
DR ProteomicsDB; 248635; -.
DR EnsemblPlants; AT2G46110.1; AT2G46110.1; AT2G46110.
DR GeneID; 819219; -.
DR Gramene; AT2G46110.1; AT2G46110.1; AT2G46110.
DR KEGG; ath:AT2G46110; -.
DR Araport; AT2G46110; -.
DR TAIR; locus:2062969; AT2G46110.
DR eggNOG; KOG2949; Eukaryota.
DR HOGENOM; CLU_036645_2_0_1; -.
DR InParanoid; O82357; -.
DR OMA; MNDMIGD; -.
DR OrthoDB; 1439584at2759; -.
DR PhylomeDB; O82357; -.
DR BioCyc; ARA:AT2G46110-MON; -.
DR BioCyc; MetaCyc:AT2G46110-MON; -.
DR UniPathway; UPA00028; UER00003.
DR PRO; PR:O82357; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82357; baseline and differential.
DR Genevisible; O82357; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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 1: Evidence at protein level;
KW Magnesium; Metal-binding; Mitochondrion; Pantothenate biosynthesis;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..347
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase 1,
FT mitochondrial"
FT /id="PRO_0000429566"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 83..84
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 36693 MW; 1A37916DA6B97795 CRC64;
MASSLTRNCS RFSKAISVRF MSNLPENTVY GGPKPQNPNQ RVTLTHLRQK HRRGEPITVV
TAYDYPSAVH LDTAGIDVCL VGDSASMVVH GHDTTLPISL DEMLVHCRAV ARGAKRPLLV
GDLPFGTYES SSSQAVDTAV RVLKEGGMDA IKLEGGSASR ITAAKAIVEA GIAVIGHVGL
TPQAISVLGG FRPQGRNIAS AVKVVETAMA LQEAGCFSVV LECVPPPVAA AATSALKIPT
IGIGAGPFCS GQVLVYHDLL GMMQHPHHAK VTPKFCKQYA NVGEVINKAL MEYKEEVSKK
VFPGPSHSPY KITASELDGF LTELQKLGFD KAASAAALAA ENMEPSK
