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Database: UniProt
Entry: B0VUG9_ACIBS
LinkDB: B0VUG9_ACIBS
Original site: B0VUG9_ACIBS 
ID   B0VUG9_ACIBS            Unreviewed;       347 AA.
AC   B0VUG9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase {ECO:0000313|EMBL:CAP02031.1};
DE            EC=2.1.1.14 {ECO:0000313|EMBL:CAP02031.1};
GN   Name=metE {ECO:0000313|EMBL:CAP02031.1};
GN   OrderedLocusNames=ABSDF2728 {ECO:0000313|EMBL:CAP02031.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP02031.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAP02031.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAP02031.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00009553}.
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DR   EMBL; CU468230; CAP02031.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VUG9; -.
DR   KEGG; abm:ABSDF2728; -.
DR   HOGENOM; CLU_040013_3_0_6; -.
DR   Proteomes; UP000001741; Chromosome.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd03311; CIMS_C_terminal_like; 1.
DR   Gene3D; 3.20.20.210; -; 1.
DR   InterPro; IPR002629; Met_Synth_C/arc.
DR   InterPro; IPR016456; Met_Synthase_cat.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR30519:SF0; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   PIRSF; PIRSF005632; Met_synth_catalytic_prd; 1.
DR   SUPFAM; SSF51726; UROD/MetE-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:CAP02031.1};
KW   Transferase {ECO:0000313|EMBL:CAP02031.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          5..329
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
SQ   SEQUENCE   347 AA;  39128 MW;  268B385BA258A46D CRC64;
     MKKLLPTSTA GSLPKPSWLA EPEKLWSPWK LENEGLIEGK KDALRLALHE QKLAGIDIVS
     DGEQTRQHFV TTFIEHLNGV DFEKRETVRI RDRYDASVPS VVGAVSRQKP VFVEDAKFLR
     QQTDQPIKWA LPGPMTMIDT LYDGHYKSRE KLAWEFAKIL NQEAKELEAA GVDIIQFDEP
     AFNVFFDEVN DWGIATLERA IEGLKCETAV HICYGYGIKA NTDWKKTLGS EWRQYEEAFP
     KLQTSNIDII SLECHNSRVP IDLLELIRGK KVMVGAIDVA TNHIETPEEV ANTLRKALQF
     VDSDKLYPCT NCGMAPLSRE VARGKLNALS AGAEIVRREL TGYDLTA
//
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