ID A0A5B8YES7_9FLAO Unreviewed; 272 AA. AC A0A5B8YES7; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 22-APR-2020, entry version 4. DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156}; DE EC=2.1.2.11 {ECO:0000256|HAMAP-Rule:MF_00156}; DE AltName: Full=Ketopantoate hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00156}; DE Short=KPHMT {ECO:0000256|HAMAP-Rule:MF_00156}; GN Name=panB {ECO:0000256|HAMAP-Rule:MF_00156, GN ECO:0000313|EMBL:QED36472.1}; GN ORFNames=FK178_01495 {ECO:0000313|EMBL:QED36472.1}; OS Antarcticibacterium sp. PAMC 28998. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Antarcticibacterium; unclassified Antarcticibacterium. OX NCBI_TaxID=2585771 {ECO:0000313|EMBL:QED36472.1, ECO:0000313|Proteomes:UP000321954}; RN [1] {ECO:0000313|EMBL:QED36472.1, ECO:0000313|Proteomes:UP000321954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PAMC 28998 {ECO:0000313|EMBL:QED36472.1, RC ECO:0000313|Proteomes:UP000321954}; RA Lee Y.M., Baek K., Lee D.-H., Shin S.C., Jin Y.K., Park Y.; RT "Antarcticibacterium arcticum sp. nov., a bacterium isolated from marine RT sediment of the Canadian Beaufort Sea."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00156, CC ECO:0000256|SAAS:SAAS00843518}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|SAAS:SAAS01125081}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00156, CC ECO:0000256|PIRSR:PIRSR000388-3}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00156, CC ECO:0000256|PIRSR:PIRSR000388-3}; CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)- CC pantoate from 3-methyl-2-oxobutanoate: step 1/2. {ECO:0000256|HAMAP- CC Rule:MF_00156}. CC -!- SUBUNIT: Homodecamer; pentamer of dimers. {ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|SAAS:SAAS00771257}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156, CC ECO:0000256|SAAS:SAAS00771239}. CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|HAMAP- CC Rule:MF_00156, ECO:0000256|SAAS:SAAS00771235}. 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; CP042476; QED36472.1; -; Genomic_DNA. DR KEGG; anp:FK178_01495; -. DR KO; K00606; -. DR UniPathway; UPA00028; UER00003. DR Proteomes; UP000321954; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule. 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 PIRSF; PIRSF000388; Pantoate_hydroxy_MeTrfase; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR TIGRFAMs; TIGR00222; panB; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|SAAS:SAAS00771250}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00156, ECO:0000256|PIRSR:PIRSR000388- KW 3, ECO:0000256|SAAS:SAAS00771249}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|PIRSR:PIRSR000388-3, ECO:0000256|SAAS:SAAS00771262}; KW Methyltransferase {ECO:0000313|EMBL:QED36472.1}; KW Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00156}; KW Reference proteome {ECO:0000313|Proteomes:UP000321954}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00156, KW ECO:0000256|SAAS:SAAS00771224, ECO:0000313|EMBL:QED36472.1}. FT REGION 52..53 FT /note="Alpha-ketoisovalerate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2" FT COILED 162..182 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 190 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-1" FT METAL 52 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-3" FT METAL 91 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-3" FT METAL 123 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-3" FT BINDING 91 FT /note="Alpha-ketoisovalerate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2" FT BINDING 121 FT /note="Alpha-ketoisovalerate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00156, FT ECO:0000256|PIRSR:PIRSR000388-2" SQ SEQUENCE 272 AA; 29763 MW; 54CE515CF067F320 CRC64; MSVAKKQYKR VTTKSLVEMK ANGEKIAMLT AYDFSMAQIV DGAGIDVILV GDSASNVMAG HETTLPITLD QMIYHAASVI RGIERSLVVV DLPFGSYQSD PKEALRSAIR IMKESGGHAV KLEGGKEIKD SVKRILNAGI PVMGHLGLTP QSIYKFGTYT VRAKEEQEAE KLKSDALLLE KMGCFALVLE KVPAKLAKEV AESLSIPVIG IGAGNGVDGQ VLVIHDMLGM NHEFNPRFLR RYADLHAVMT KAFEDYRDDV KSSSFPSDEE QY //