ID A0A0N1MVJ3_9GAMM Unreviewed; 355 AA.
AC A0A0N1MVJ3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000313|EMBL:KPH63735.1};
GN ORFNames=ADS77_07375 {ECO:0000313|EMBL:KPH63735.1};
OS Pseudoalteromonas porphyrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=187330 {ECO:0000313|EMBL:KPH63735.1, ECO:0000313|Proteomes:UP000037848};
RN [1] {ECO:0000313|EMBL:KPH63735.1, ECO:0000313|Proteomes:UP000037848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-SED14 {ECO:0000313|EMBL:KPH63735.1,
RC ECO:0000313|Proteomes:UP000037848};
RA Coil D.A., Jospin G., Lee R.D., Eisen J.A.;
RT "Draft Genome Sequence of Pseudoalteromonas porphyrae UCD-SED14.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KPH63735.1}.
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DR EMBL; LHPH01000007; KPH63735.1; -; Genomic_DNA.
DR RefSeq; WP_054205570.1; NZ_LITL01000015.1.
DR AlphaFoldDB; A0A0N1MVJ3; -.
DR STRING; 187330.AMS58_13520; -.
DR PATRIC; fig|187330.3.peg.3504; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000037848; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
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}; 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..329
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 314
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"
SQ SEQUENCE 355 AA; 38790 MW; 93C66EEF837161E8 CRC64;
MPNNLENKSA ELIDALKQRI LILDGAMGTM IQEHKLEEED YRGERFKDWH VLIKGNNDLL
SLTQPKIIGD IHRGFLSAGA DIIETNTFNS TTISMEDYDM ASISREVNLE SAKLARSICD
EFTAKNPAKP RYVAGVLGPT SKTCSISPDV NDPGYRNVTF DKLVTAYVES TLALMEGGAD
LILIETIFDT LNAKAASFAV EEAFEQAGRK LPVMISGTIT DASGRTLSGQ TTEAFYNSIR
HIKPISIGLN CALGPDLLRQ YVEELSRVCE TFTSVHPNAG LPNEFGEYDL EAPEMAAEII
DWGKSGFINI VGGCCGTTPA HIRAFAKGLE GVKPRPLPEL EVRMRLSGLE ACNLN
//
