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Database: UniProt
Entry: F8FI22_PAEMK
LinkDB: F8FI22_PAEMK
Original site: F8FI22_PAEMK 
ID   F8FI22_PAEMK            Unreviewed;       766 AA.
AC   F8FI22;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00172};
DE            EC=2.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00172};
DE   AltName: Full=Cobalamin-independent methionine synthase {ECO:0000256|HAMAP-Rule:MF_00172};
DE   AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000256|HAMAP-Rule:MF_00172};
GN   Name=metE {ECO:0000256|HAMAP-Rule:MF_00172,
GN   ECO:0000313|EMBL:AEI43364.1};
GN   OrderedLocusNames=KNP414_04838 {ECO:0000313|EMBL:AEI43364.1};
OS   Paenibacillus mucilaginosus (strain KNP414).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI43364.1, ECO:0000313|Proteomes:UP000006620};
RN   [1] {ECO:0000313|Proteomes:UP000006620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620};
RA   Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEI43364.1, ECO:0000313|Proteomes:UP000006620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNP414 {ECO:0000313|EMBL:AEI43364.1,
RC   ECO:0000313|Proteomes:UP000006620};
RX   PubMed=24158556;
RA   Lu J.J., Wang J.F., Hu X.F.;
RT   "Genome Sequence of Growth-Improving Paenibacillus mucilaginosus Strain
RT   KNP414.";
RL   Genome Announc. 1:e00881-13(2013).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC       methyltetrahydrofolate to homocysteine resulting in methionine
CC       formation. {ECO:0000256|ARBA:ARBA00002777, ECO:0000256|HAMAP-
CC       Rule:MF_00172}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC         methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC         ChEBI:CHEBI:58207; EC=2.1.1.14; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00172};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00172};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00172};
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, ECO:0000256|HAMAP-Rule:MF_00172}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00009553, ECO:0000256|HAMAP-
CC       Rule:MF_00172}.
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DR   EMBL; CP002869; AEI43364.1; -; Genomic_DNA.
DR   RefSeq; WP_013918517.1; NC_015690.1.
DR   AlphaFoldDB; F8FI22; -.
DR   KEGG; pms:KNP414_04838; -.
DR   PATRIC; fig|1036673.3.peg.4454; -.
DR   HOGENOM; CLU_013175_0_0_9; -.
DR   OMA; KVMKGML; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000006620; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_00172}; Repeat {ECO:0000256|HAMAP-Rule:MF_00172};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00172};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00172}.
FT   DOMAIN          4..312
FT                   /note="Cobalamin-independent methionine synthase MetE N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08267"
FT   DOMAIN          429..751
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
FT   ACT_SITE        697
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-3"
FT   BINDING         16..19
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         19
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         112
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         117
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         434..436
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         434..436
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         487
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         487
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         518..519
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         564
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         602
FT                   /ligand="L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:58199"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         602
FT                   /ligand="L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:57844"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172,
FT                   ECO:0000256|PIRSR:PIRSR000382-1"
FT   BINDING         608
FT                   /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58207"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         644
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         644
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         646
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         646
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         668
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         668
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         729
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00172"
FT   BINDING         729
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   766 AA;  85688 MW;  040CB15B701CDB12 CRC64;
     MVRSSVLGYP RIGVHREWKK ALEAFWSGRL GESGLHEELQ AIRLDHLRRL KEKGIHLIPV
     NDFSYYDHVL DTAVMFGIVP RRFGYTGGAV PLSTYYGIAR GLKDAPAGEM TKWFNTNYHY
     IVPELDGAEP VLTENKPLLA YREAREKLGI SGKPVLLGPL TFLKLSKGYA ERDTDAWIGR
     LLPLYVQVLR ELAEEGAEWV QLDEPVLVTN VSEADVQRLK RIYETFASAV PGIRIMLQTY
     FESLEHYRDI IRLPVQGIGL DFVHGGEGNL SSIRAHGFPE DKVLGAGVID GRGIWRAPLS
     GKLKLLRELS EFVSPERLIV QTSCSLLHVP VTTKGETELP AGLKNALAFA DEKLEEVVLL
     ARALADGGAA DDASLDAADL ALDLLQRSPE RSRRDIQQAV AAILDQPIER SPFAVRQTEQ
     RKKWKLPLFP TTTIGSFPQS AEVRAARQSW RRGEWSGEQY AGFIRGQIDR WIDLQEEIGL
     DVLVHGEFER TDMVEFFGEK LAGFAFTRNG WVQSYGSRCV KPPIIYGDTA FVKPMTVEET
     KYAQSRTPRP VKGMLTGPIT ILNWSFVRDD LPREEIAYQL AYALRQEVEA LERAGIGMIQ
     VDEPAVREGL PLKEAEHAAY LAWAVRAFRL ATCSVQDTTQ IHTHMCYCDF HDMIGSIEAM
     DADVISIETS RSHGELIGSF ETNTYRLGIG LGVYDIHSPR IPPVEEMTSM VERALRVLEP
     GLFWINPDCG LKTRGAEETA ASLRHMVEAA RIVRAKYEGK AGALLP
//
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