ID A0A077ZBV6_TRITR Unreviewed; 519 AA.
AC A0A077ZBV6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|ARBA:ARBA00012618};
DE EC=2.1.2.11 {ECO:0000256|ARBA:ARBA00012618};
GN ORFNames=TTRE_0000560001 {ECO:0000313|EMBL:CDW57309.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW57309.1};
RN [1] {ECO:0000313|EMBL:CDW57309.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW57309.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000344};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005033}.
CC -!- SIMILARITY: Belongs to the PanB family.
CC {ECO:0000256|ARBA:ARBA00008676}.
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DR EMBL; HG806148; CDW57309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZBV6; -.
DR STRING; 36087.A0A077ZBV6; -.
DR UniPathway; UPA00028; UER00003.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:InterPro.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06557; KPHMT-like; 1.
DR CDD; cd00560; PanC; 1.
DR Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR HAMAP; MF_00156; PanB; 1.
DR HAMAP; MF_00158; PanC; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR003700; Pantoate_hydroxy_MeTrfase.
DR InterPro; IPR003721; Pantoate_ligase.
DR InterPro; IPR042176; Pantoate_ligase_C.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR00222; panB; 1.
DR NCBIfam; TIGR00018; panC; 1.
DR PANTHER; PTHR20881; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR20881:SF0; 3-METHYL-2-OXOBUTANOATE HYDROXYMETHYLTRANSFERASE; 1.
DR Pfam; PF02569; Pantoate_ligase; 1.
DR Pfam; PF02548; Pantoate_transf; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:CDW57309.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 519 AA; 56531 MW; B26F3C9BDD9C57B1 CRC64;
MQKQKEQGDK ISMLTAYDYS TAKLMDQAGI NSLLVGDSLG MVMLGYEDTL SVTMEDMIHH
SRAVANGAQN ALVVTDLPFM SYHISIPDAV ANAGRLIKEG HAAAVKLEGG EAFSETIQAI
TRASIPVMGH IGLTPQSIHA FGGFKVQGKT IEAAQKILQD ALAVEKAGAF AIVLEAIPAD
LAALITKKLT IPTIGIGAGN QTDGQVLVYQ DMLGMYGEMQ PKFYRTGNHR SIGERNKTLK
TVKTIEEVRN QVKAWRQAGQ SIGFVPTMGA LHEGHRSLME KAKQDNDHVI VSIFVNPTQF
SPNEDLASYP RKLQADQALC SAAGVALIFH PEVEEMYPAG FNTYVESFGV TEVLEGASRP
AHFRGVTTVV LKLIQITQPD RVYFGQKDAQ QVAVVQQMTR DLNIPVDIIA CPIIREADGL
AKSSRNSYLN PAERQAALVL SRALKLAQEQ LSAGVRNSQA LIQAMTAEIA SEPLAKIDYI
EIVNQKTLQK VDTIDSAILV PIAVYIGKTR LIDNFYWEE
//
