ID G8NVM1_GRAMM Unreviewed; 627 AA.
AC G8NVM1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Methionine synthase., Methylenetetrahydrofolate reductase (NAD(P)H) {ECO:0000313|EMBL:AEU37693.1};
DE EC=1.5.1.20 {ECO:0000313|EMBL:AEU37693.1};
DE EC=2.1.1.13 {ECO:0000313|EMBL:AEU37693.1};
GN OrderedLocusNames=AciX8_3395 {ECO:0000313|EMBL:AEU37693.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU37693.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU37693.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX8 {ECO:0000313|EMBL:AEU37693.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) 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; CP003130; AEU37693.1; -; Genomic_DNA.
DR RefSeq; WP_014266567.1; NC_016631.1.
DR AlphaFoldDB; G8NVM1; -.
DR STRING; 682795.AciX8_3395; -.
DR KEGG; gma:AciX8_3395; -.
DR eggNOG; COG0646; Bacteria.
DR eggNOG; COG0685; Bacteria.
DR HOGENOM; CLU_453272_0_0_0; -.
DR OrthoDB; 9803687at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000007113; 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; PTHR11103:SF18; HOMOCYSTEINE S-METHYLTRANSFERASE 1-RELATED; 1.
DR PANTHER; PTHR11103; SLR1189 PROTEIN; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEU37693.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 2..295
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 627 AA; 67201 MW; 117459682327717B CRC64;
MAVGIDRLFA GGTVLCDGAM GTMLYSCGVF INRCYDELNL SQPEMVRSVH QQYLQAGAEV
IETNTFGANS FRLERFALRE KVREFNLAGA AIARQSVDAI REKQGTEAFV AGAVGPLGVR
LEPLGKLSLE EAREAFAEQI SALAEGGVDL IIIETMMSID EAEQAVLAAR QVAPHLKVAV
MVTVDEDGNC LDGTSPEVAA ERLTAVGADA IGCNCSSGPA TVLTVIERMR EATALPLLAM
PNAGMPRNVE GRNIYLTSPE YMASFVRKAV RAGASWVGGC CGTTPAHIRA MRGSLRAMDA
QESGERATEH TPHIVHASES EHRVEPRPLG ERSQIGRMIA DGEFVTMVEI VPPKGFDCSK
ELAGALLMKK RGVHVINVPD SPRASARMGA QSLCVQIQQQ VGIETILHYT CRDRNVLSMQ
SDLLGASSIG LKNILCLTGD PPKMGNYPDA TAVFDVDAIG LVNIVHGLNQ GLDIGRNPIG
GSTGFTISVA ANPGVPDIEH EVRRFAYKVE AGAEFCITQP VFDLRLLEDF LRRIEGFRIP
VIAGIWPLTS LRNAEFMKND LRVAMPDEIF VRMAAAGGKE EALAEGLKIA QEMLASVRGS
VQGVQVSAPF GKYTAAAEVL GLTEEIA
//
