ID K1VYW4_TRIAC Unreviewed; 1818 AA.
AC K1VYW4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase {ECO:0000256|RuleBase:RU362100};
DE EC=2.1.2.11 {ECO:0000256|RuleBase:RU362100};
GN ORFNames=A1Q2_00962 {ECO:0000313|EMBL:EKD04732.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD04732.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD04732.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04732.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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|RuleBase:RU362100}.
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 ECO:0000256|RuleBase:RU362100};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005033, ECO:0000256|RuleBase:RU362100}.
CC -!- SIMILARITY: Belongs to the PanB family. {ECO:0000256|ARBA:ARBA00008676,
CC ECO:0000256|RuleBase:RU362100}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD04732.1}.
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DR EMBL; AMBO01000191; EKD04732.1; -; Genomic_DNA.
DR STRING; 1220162.K1VYW4; -.
DR eggNOG; KOG1956; Eukaryota.
DR eggNOG; KOG2539; Eukaryota.
DR eggNOG; KOG2949; Eukaryota.
DR HOGENOM; CLU_237687_0_0_1; -.
DR InParanoid; K1VYW4; -.
DR OrthoDB; 166270at2759; -.
DR UniPathway; UPA00028; UER00003.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd06557; KPHMT-like; 1.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 2.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 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 InterPro; IPR015324; Ribosomal_Rsm22-like.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR010666; Znf_GRF.
DR NCBIfam; TIGR00222; panB; 1.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF02548; Pantoate_transf; 1.
DR Pfam; PF09243; Rsm22; 2.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362100};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362100};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 2..123
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 657..698
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 320..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1818 AA; 199811 MW; 81BBAB1EEEE1E837 CRC64;
MKVLCVAEKP SIAKSITAIL SENNFTSRQS GHQYIRNYDF DYNLPPPLGG GRGTDFTVTS
VLGHLTSLDM KRVETNLKNE ARRAQILMIW TDCDREGEHI GSEIESVCRR SNPNITVKRA
RFSAIIAAQI HQACRQAGNL DENQAKAVEA RTELDLRIGA AFTRFLTQTL QIRVPELGDQ
KLVSYGPCQF PTLGFVVDQY NRVQSFVPEQ FWYISVTCER DSDDGETFKV EFKWRRNHLF
DLDVAVLLSD FRKPLPLTTV DLQQSGSRLL GMTPKRILDK GFLSYPRTET DQYDKAFDFM
ALIRKQELNR ELLDGAFQTP RNGRKNDKAH PPIHPTNGAQ GLEGEERKVY EFVTRRFLAS
CSKNAEGMQT TVEIEIAGEY FHASGVIVKA RNYLEVYPYD KWNSNPIPDF QEGEQFVPDE
CMLKEGVTTA PNYLTEADLV GLMDKNGIGT DATIADHIAK IIDREYVLTK TQQKTKYLVP
SMLGIGLVEG FNAIGFDRSL SKPHLRRETE HRMQLICDGQ QRKGEVIDLS LEEYREVYVK
AKREFNTVVD SVKNYLHGEG EAQEALRAAA RGGRGARGGT RGTRGTRGTR GGRGGGRGAV
PRGSPDYDDD DDDDFGGPPR GGGAVRGSST RGPGTAPAPT RGTTRALADG DNEPPCCQCG
TPAVQRTSNS AANPGRQFYA CPKPRDEQCG FFLGAPGEEG GHTVKRPEVQ LEEEATGAAS
SVAKRATGQA SVPTKVAAHK AVGQTTRLAE LPGQDASSAA RKDTGPAIAR TSRTVEGTLV
VPHAVAAALA VGPRVAAVGD EGVAAVEAEA EEMPKEKQSI VDEPPHTEPI LDPSFAALMN
DVNMSLKRAK QGEKSYVAEK DITPVPASEQ PAEVEEGEED AQSPRRPPRR SPAAMFGTKN
IGMIVLPDWL IEGVQNEVEQ VDNRRIVREK YLEMLEPKKE KSDKTNSRNT EQHALARAAA
FLPAQCAAVA NVLRELRTRV GDIKGPILET TDGIAPGLWA ATEELGVDAI REFTLIQRTR
WGLALAERLA QPLAIDVNLD EMDFKRDISF AGLPQPPQVA MSTFMMSMLP TAQSRRDHLK
QLLETDAEHI VIVDRGSTEV WEAMDAARTF LMEHSTPEHP LHITAPCPHQ FTCPRAGTRE
ACSFIQKVQR PPFLRRTKHA KRGEENITYS YLIISRGERP KSTATAGRFG IVAAELEAKK
KAKATKRPEL VPVEGGESGA FEVVNTAAME YEVPPAESLD DPALVQSLRE QAYSWPRLIA
QPMKRSGHVV MDMCAPSGNL ERRRYAKSTG KQEYYDARRT AWGDLFPHES KAKIEVRDRG
IIHLKKTLSE AELIEQERDI KRKEKAKREA AKLAANTGKA PPPPPLEPAE PAQSVYAEPR
TVKGKNGLAF ESTGDPELDA LYKQLGIAPV VAEPVMGSPE GMTEEEEMEQ ELERMFGTFD
PLPAEPEPMP TSKRGRRQAE AELTDVRFSR RGRQRRPKAW ERAKERGERE YSTSAFALGR
RPMSTLARPA VSQTGLGVQK RFMSARPAEL KGRPKLTVGA LQKQYASGTP ISVLTAYDYP
TSRLCADAEV DIILVGDSLA QVALGYQSTT ELTLSEMCHH IRAVRRGSGS SFILADMPFG
SFEASVEEGV KSAVELVKAG ADAVKIEGGA ETLPLVRRLT SFGIAVMPHI GLMPQRAAST
GYRVQGKQAS AALDLIQLAR DFEAAGAFGL LLEAIPHQLG ALITAKVGIP TIGIGAGNQT
SGQVLVLTDL LGTYGFDADC KAPKFVRLYA QSGQKESDAV RQYIADVRDR SFPKTGEETY
TMPEKELGEL RRLVDEMD
//
