ID I3ZIA8_TERRK Unreviewed; 623 AA.
AC I3ZIA8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Cobalamin-dependent methionine synthase I {ECO:0000313|EMBL:AFL88976.1};
GN OrderedLocusNames=Terro_2740 {ECO:0000313|EMBL:AFL88976.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL88976.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL88976.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777}.
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DR EMBL; CP003379; AFL88976.1; -; Genomic_DNA.
DR RefSeq; WP_014786240.1; NC_018014.1.
DR AlphaFoldDB; I3ZIA8; -.
DR STRING; 926566.Terro_2740; -.
DR KEGG; trs:Terro_2740; -.
DR eggNOG; COG0646; Bacteria.
DR eggNOG; COG0685; Bacteria.
DR HOGENOM; CLU_453272_0_0_0; -.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006056; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006555; P:methionine metabolic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00537; MTHFR; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR InterPro; IPR003171; Mehydrof_redctse-like.
DR PANTHER; PTHR45833:SF2; BIFUNCTIONAL HOMOCYSTEINE S-METHYLTRANSFERASE_5,10-METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR Pfam; PF02219; MTHFR; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR PROSITE; PS50970; HCY; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006056};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 10..300
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 623 AA; 66155 MW; 8FC01CC43CE09976 CRC64;
MSETKTQPQT HDVERLFGPA PVLCDGAMGT MFYARGIFIN RCFDELNLTD PQMVRDLHEE
YLVAGAEVIE TNTFGANAVR LKRFGLEGKV AEINTAAVRI ARAAVDGVRE KHAHQAFVAG
ALGSLGFDKK DADPAMMLAA YREQVDALVA AGVDLFVVET VTSMAQAKAA IQAARDAAPD
LPVIAMVTVT DAGIVADGTS PEDAARLFEE WGARAVGCNC SDGPMQVLDT IERMRKVTKL
PIAAMPNAGL PNCVDGRSIY LSSPEYLASF ARKAMRLGAT LIGGCCGTTP KHIKAMRSSV
KAIQAQAEGV LSAGAKPTAS EIAPPPLAER SLIGARIARG EFVSMVEIVP PKGIDATREL
EGARMLKQLG VHAINVPDSP RASTRMSAGS MCLQIEQKVG IEAVIHYTCR DRNLLGIQSD
LLGASSLGLR NILCLTGDPP KMGSYPDATA VFDVDAVGLT RIVRDMNHGL DIGGASIGSS
TGFVIAVAAN PGVPDLDAEV RRFAAKVEAG AEFGITQPVF DMRLLETFLK RIEGFRIPIV
AGIWPLTSVK NAEFMKNDLK VSMPDEILSR MAANAASPEH SRAEGIRIAQ EMLAEAQGMV
QGVQVSAPFA RYAAAAEVLE AML
//
