ID BHMT1_DANRE Reviewed; 400 AA.
AC Q32LQ4; Q5PSM1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-APR-2013, entry version 60.
DE RecName: Full=Betaine--homocysteine S-methyltransferase 1;
DE EC=2.1.1.5;
GN Name=bhmt; ORFNames=wu:fb53h01, zgc:123027;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lapek J.D. Jr., Warren J.T. Jr.;
RT "Molecular genetic analysis of folate metabolism in the zebrafish.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of homocysteine metabolism.
CC Converts betaine and homocysteine to dimethylglycine and
CC methionine, respectively. This reaction is also required for the
CC irreversible oxidation of choline (By similarity).
CC -!- CATALYTIC ACTIVITY: Trimethylammonioacetate + L-homocysteine =
CC dimethylglycine + L-methionine.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Amine and polyamine degradation; betaine degradation;
CC sarcosine from betaine: step 1/2.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC novo pathway; L-methionine from L-homocysteine (BhmT route): step
CC 1/1.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Contains 1 Hcy-binding domain.
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DR EMBL; AY830415; AAV74219.1; -; mRNA.
DR EMBL; BC109472; AAI09473.1; -; mRNA.
DR IPI; IPI00491662; -.
DR RefSeq; NP_001012498.1; NM_001012480.1.
DR UniGene; Dr.75610; -.
DR ProteinModelPortal; Q32LQ4; -.
DR SMR; Q32LQ4; 7-393.
DR STRING; 7955.ENSDARP00000040421; -.
DR GeneID; 322228; -.
DR KEGG; dre:322228; -.
DR CTD; 635; -.
DR ZFIN; ZDB-GENE-030131-947; bhmt.
DR eggNOG; COG0646; -.
DR HOGENOM; HOG000231636; -.
DR HOVERGEN; HBG080367; -.
DR KO; K00544; -.
DR OrthoDB; EOG4001JM; -.
DR UniPathway; UPA00051; UER00083.
DR UniPathway; UPA00291; UER00432.
DR NextBio; 20807724; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:EC.
DR GO; GO:0008898; F:homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006579; P:amino-acid betaine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.330; -; 1.
DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR InterPro; IPR003726; S_MeTrfase.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037505; Betaine_HMT; 1.
DR SUPFAM; SSF82282; S_methyl_trans; 1.
DR PROSITE; PS50970; HCY; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Cytoplasm; Metal-binding; Methyltransferase;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1 400 Betaine--homocysteine S-methyltransferase
FT 1.
FT /FTId=PRO_0000273221.
FT DOMAIN 8 309 Hcy-binding.
FT METAL 212 212 Zinc (By similarity).
FT METAL 294 294 Zinc (By similarity).
FT METAL 295 295 Zinc (By similarity).
FT CONFLICT 189 189 H -> P (in Ref. 1; AAV74219).
FT CONFLICT 192 192 I -> T (in Ref. 1; AAV74219).
FT CONFLICT 224 224 A -> V (in Ref. 1; AAV74219).
SQ SEQUENCE 400 AA; 44066 MW; A6A3A9A824D5D26A CRC64;
MAPVGSKRGV LERLNAGEVV IGDGGFVFAL EKRGYVKAGP WTPEAAAEHP EAVRQLHREF
LRAGSNVMQT FTFYASDDKL ENRGNKLSFT GQQINEAACD LAREVANEGD ALVAGGVSQT
PSYLSCKSEE EVKKTFKKQL DVFIKKNVDL LIAEYFEHVE EAEWAVQVLK ATGKPVAATL
CIGPDGDMHG VIPGECAVRL VKAGADIVGV NCHFDPLTCV KTVAMMKAAV EKAGLKAHYM
TQPLAYHTPD CSCQGFIDLP EFPFALEPRI LTRWEMQQYA REAYKAGIRY IGGCCGFEPY
HIRAVAEELS AERGFLPEAS QKHGLWGSGL EMHTKPWVRA RARRDYWEKL KPASGRPLCP
SMSTPDGWGV TRGHAALMQQ KEATTAEQLR PLFQQADAKH
//