ID Q12H55_POLSJ Unreviewed; 348 AA.
AC Q12H55;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Methionine synthase (B12-dependent) {ECO:0000313|EMBL:ABE42137.1};
DE EC=2.1.1.13 {ECO:0000313|EMBL:ABE42137.1};
GN OrderedLocusNames=Bpro_0172 {ECO:0000313|EMBL:ABE42137.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE42137.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; CP000316; ABE42137.1; -; Genomic_DNA.
DR RefSeq; WP_011481147.1; NC_007948.1.
DR AlphaFoldDB; Q12H55; -.
DR STRING; 296591.Bpro_0172; -.
DR KEGG; pol:Bpro_0172; -.
DR eggNOG; COG0646; Bacteria.
DR HOGENOM; CLU_004914_3_0_4; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR PROSITE; PS50970; HCY; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 9..330
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 348 AA; 37863 MW; A5D5F43F3A3A347D CRC64;
MKPLNYTRGQ QLPAILEQRI AILDGAMGTM IQRFKLNEAQ YRGERFKDFH KDVKGNNELL
SLTRPDVIRD IHEGYLAAGA DMIETNTFGA TTVAQADYDM ADLAVEMNYE SARIARAACD
KFSTPDKPRF VVGALGPTPK TASISPDVND PGARNTSFEE LRKAYYEQTE ALVKGGSDVL
LVETIFDTLN AKAALFAIDE YFDNSGECLP LIISGTVTDA SGRILSGQTV TAFWHSVRHA
RPLAIGLNCA LGATLMRPYI QELARVAGDT FISCYPNAGL PNPMSDTGFD ETPDVTSRLL
REFADEGLVN IVGGCCGTTP EHIQAIAHAV APLPSRAVAS RFFYREAA
//
