PANB2_ARATH
ID PANB2_ARATH Reviewed; 354 AA.
AC Q9M315;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
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; OrderedLocusNames=At3g61530;
GN ORFNames=F2A19.130;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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}.
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; AL132962; CAB71083.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80218.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80219.1; -; Genomic_DNA.
DR EMBL; BT025255; ABF19008.1; -; mRNA.
DR EMBL; AY087528; AAM65070.1; -; mRNA.
DR PIR; T47945; T47945.
DR RefSeq; NP_191712.1; NM_116018.4.
DR RefSeq; NP_974474.1; NM_202745.4.
DR AlphaFoldDB; Q9M315; -.
DR SMR; Q9M315; -.
DR BioGRID; 10640; 3.
DR IntAct; Q9M315; 1.
DR STRING; 3702.AT3G61530.2; -.
DR PaxDb; Q9M315; -.
DR PRIDE; Q9M315; -.
DR ProteomicsDB; 248655; -.
DR EnsemblPlants; AT3G61530.1; AT3G61530.1; AT3G61530.
DR EnsemblPlants; AT3G61530.2; AT3G61530.2; AT3G61530.
DR GeneID; 825326; -.
DR Gramene; AT3G61530.1; AT3G61530.1; AT3G61530.
DR Gramene; AT3G61530.2; AT3G61530.2; AT3G61530.
DR KEGG; ath:AT3G61530; -.
DR Araport; AT3G61530; -.
DR TAIR; locus:2082847; AT3G61530.
DR eggNOG; KOG2949; Eukaryota.
DR HOGENOM; CLU_036645_2_0_1; -.
DR InParanoid; Q9M315; -.
DR OMA; VLVWTDM; -.
DR OrthoDB; 1439584at2759; -.
DR PhylomeDB; Q9M315; -.
DR UniPathway; UPA00028; UER00003.
DR PRO; PR:Q9M315; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M315; baseline and differential.
DR Genevisible; Q9M315; 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:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
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..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..354
FT /note="3-methyl-2-oxobutanoate hydroxymethyltransferase 2,
FT mitochondrial"
FT /id="PRO_0000429567"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 85..86
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="3-methyl-2-oxobutanoate"
FT /ligand_id="ChEBI:CHEBI:11851"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 37364 MW; E8CF63A1D0BCB4DA CRC64;
MAASLVRSCC SRASRAITTV RFMSNVPEDT VYGGPKPQNS NQRVTLTQLR QKHRKGEPIT
MVTAYDYPSA VHIDTAGIDV CLVGDSAAMV VHGYDTTLPI SLEEMLVHCR AVARGAKRPL
LVGDLPFGTY ESSTNQAVDT AVRVLKEGGM DAIKLEGGSP SRITAAKSIV EAGIAVMGHV
GLTPQAISVL GGFRPQGKNI ASAVKVVETA MALQEAGCFS VVLECVPPPV AAAATSALNI
PTIGIGAGPF CSGQVLVYHD LLGMMQHPHH AKVTPKFCKQ YAQVGEVINK ALLEYKEEVS
KHLFPGPSHS PYKISSSDLD GFLSELQKLG LDKAASDAAA SAEKMDHSDS PSSQ
