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Database: UniProt
Entry: K7RZV7_TEPAE
LinkDB: K7RZV7_TEPAE
Original site: K7RZV7_TEPAE 
ID   K7RZV7_TEPAE            Unreviewed;       268 AA.
AC   K7RZV7; F4LTH4;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Putative methyltransferase {ECO:0000313|EMBL:AFV95336.1};
GN   Name=acsE {ECO:0000313|EMBL:AFV95336.1};
GN   OrderedLocusNames=TEPIRE1_0337 {ECO:0000313|EMBL:CCP25014.1};
OS   Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Tepidanaerobacteraceae; Tepidanaerobacter.
OX   NCBI_TaxID=1209989 {ECO:0000313|EMBL:AFV95336.1};
RN   [1] {ECO:0000313|EMBL:CCP25014.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Re1 {ECO:0000313|EMBL:CCP25014.1};
RA   Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT   "First Genome Sequence of a Syntrophic Acetate-Oxidizing Bacterium,
RT   Tepidanaerobacter acetatoxydans Strain Re1.";
RL   Genome Announc. 1:e00213-e00212(2013).
RN   [2] {ECO:0000313|Proteomes:UP000010802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX   PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA   Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT   "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT   Tepidanaerobacter acetatoxydans strain Re1.";
RL   Genome Announc. 1:E00213-E00213(2013).
RN   [3] {ECO:0000313|EMBL:AFV95336.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Re1 {ECO:0000313|EMBL:AFV95336.1};
RX   PubMed=23239474; DOI=10.1002/mbo3.50;
RA   Muller B., Sun L., Schnurer A.;
RT   "First insights into the syntrophic acetate-oxidizing bacteria--a genetic
RT   study.";
RL   MicrobiologyOpen 2:35-53(2013).
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
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DR   EMBL; JQ979073; AFV95336.1; -; Genomic_DNA.
DR   EMBL; HF563609; CCP25014.1; -; Genomic_DNA.
DR   RefSeq; WP_013777428.1; NC_019954.2.
DR   AlphaFoldDB; K7RZV7; -.
DR   STRING; 1209989.TepRe1_0302; -.
DR   KEGG; tae:TepiRe1_0337; -.
DR   KEGG; tep:TepRe1_0302; -.
DR   PATRIC; fig|1209989.3.peg.352; -.
DR   eggNOG; COG1410; Bacteria.
DR   HOGENOM; CLU_070996_0_0_9; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000010802; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   PANTHER; PTHR45833:SF2; BIFUNCTIONAL HOMOCYSTEINE S-METHYLTRANSFERASE_5,10-METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AFV95336.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFV95336.1}.
FT   DOMAIN          1..245
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   268 AA;  29763 MW;  10F6F8E39857D15B CRC64;
     MIIIGEKING TIPSVKKAIE EKDEKIIHDL AVRQADAGAD YIDVCAGTTP EIEVETLKWL
     MSIVQDATDK PLCIDSPNPR TIETVFGYAR KPGIINSVSL EGDKCEVIYP LIQGTDWQVI
     ALTCDNKGIP SDVKTRIDIT EALVERAEKY GITPDRIHID PLVIALATDN QSLIKFIETM
     KIIKAKYNNI KITSGLSNIS FGMPLRRVIN QTFLTLAIYA GMDSAIMDPC NRDMMATLLA
     TEALLGRDRY CRKFTNAYRK GKIGPKKD
//
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