ID A0A139I8J9_9PEZI Unreviewed; 769 AA.
AC A0A139I8J9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000256|ARBA:ARBA00012034};
DE EC=2.1.1.14 {ECO:0000256|ARBA:ARBA00012034};
GN ORFNames=AC579_8548 {ECO:0000313|EMBL:KXT11071.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT11071.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT11071.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT11071.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000256|ARBA:ARBA00002777}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000382-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR000382-
CC 2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004681}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00009553}.
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:KXT11071.1}.
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DR EMBL; LFZO01000221; KXT11071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I8J9; -.
DR STRING; 113226.A0A139I8J9; -.
DR UniPathway; UPA00051; UER00082.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR CDD; cd03312; CIMS_N_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
DR HAMAP; MF_00172; Meth_synth; 1.
DR InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR NCBIfam; TIGR01371; met_syn_B12ind; 1.
DR PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR30519:SF0; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; UROD/MetE-like; 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000382-2};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000382-2}.
FT DOMAIN 4..321
FT /note="Cobalamin-independent methionine synthase MetE N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08267"
FT DOMAIN 439..762
FT /note="Cobalamin-independent methionine synthase MetE C-
FT terminal/archaeal"
FT /evidence="ECO:0000259|Pfam:PF01717"
FT ACT_SITE 708
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-3"
FT BINDING 19
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 120
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 444..446
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 444..446
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 497
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 528..529
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 574
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 612
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 612
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
FT BINDING 740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR000382-2"
SQ SEQUENCE 769 AA; 86974 MW; 73092883D3124316 CRC64;
MVQSSVLGFP RMGKLRDLKK ANEAYWADKL SRDELLAEGK RLRLEHWKIQ KDAGVDIIPS
NDFSYYDHVL DHIQMFSAVP ERYSKHNLHA IDEYFAMGRG HQKENVDVPS LEMVKWFDSN
YHYVKPTLQD NQTFKLVDNA KPIAEFNEAK EAGIVTRPVI LGPVSFLHLG KADRGSSVDT
ITLLDKLLPV YEELLTQLKA AGAETVQIDE PVLVFDLPKK TRDAFKPAYE KLTALQGSKG
PQLVLATYFG DVIHNFDVID AALTGTYAFH VDLVRHPEQL AKVVEHLGPK QVLSAGVVDG
RNIWKTNFKN AIEILETAIQ KLGKERVIVA TSSSLLHTPH TLASEKNLDD EVRDWFSFAS
EKAIEIAILA KAVTEGPDAV RSQLEANAAS MQSRATSKRT NNPAVKERMA AVKKEDYERK
SGFPTRYEAQ KKHLNLPIFP TTTIGSFPQT KEIRIQRNKF TKGEITPEEY EKFIEKEIDE
VVRIQEELGL DVLVHGEPER NDMVQYFGER LDGYVFTTHA WVQSYGSRCV RPPILVGDVS
RPAPMTVKES KYAASVSKKP MKGMLTGPIT CLRWSFPRDD VHQSIQAAQL ALALRDEVVD
LEKAGVYVIQ VDEPALREGL PLRAGSEREN YLQWAVDSFK LSTAGVEDST QIHSHFCYSE
FQDFFHAIAA LDADVLSIEN SKSDAKLLKV FIDEAYPRHI GPGVYDIHSP RVPSEQEIKD
RIQEMLQYLK PDQLWINPDC GLKTRQWKET KAALVNMVNA AKHFREQQK
//
