※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||||||
Theoretical PI | 5.47 | ||||||||||||||||||||||||||||||||||
Molecular Weight | 137038.79 | ||||||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||||||
Protein Name | Cobalamin-dependent methionine synthase | ||||||||||||||||||||||||||||||||||
Gene Name | METH1; CHLREDRAFT_76715 | ||||||||||||||||||||||||||||||||||
Created Date | 2007-12-04 | ||||||||||||||||||||||||||||||||||
Organism | Chlamydomonas reinhardtii(Chlamydomonas smithii) | ||||||||||||||||||||||||||||||||||
NCBI Taxa ID | 3055 | ||||||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Sequence Annotation region of interest 836 837 Cobalamin-binding region of interest 1205 1206 S-adenosyl-L-methionine binding metal ion-binding site 237 Zinc metal ion-binding site 300 Zinc metal ion-binding site 301 Zinc metal ion-binding site 761 Cobalt (cobalamin axial ligand) binding site 956 S-adenosyl-L-methionine binding site 1150 S-adenosyl-L-methionine; via carbonyl oxygen binding site 1154 Cobalamin; via carbonyl oxygen Keyword Cobalamin,Cobalt,Complete proteome,Metal-binding,Methyltransferase,Reference proteome,S-adenosyl-L-methionine,Transferase,Zinc Sequence Source UniProt Protein Sequence MRERIIFIDG AMGTQIQKFT LEEEDFRGER YAKHSHELKG NNDLLVITRP DVISKIHTAY 60 LEAGADIIET NTFNGTWISQ SDYELQADVA LINRTAAQLA KKCVADFLAK NPGSGPRFVA 120 GAIGPTNKTL SVSPSVENPA FRGITYDEVV DAYYKQAEAL VEGGVDMFLV ETIFDTLNAK 180 AAMYALEKFF SDKGMRLPVF VSGTIVDNSG RTLSGQTNEA FWNSIRHAKP MAVGLNCALG 240 AKDMLKYVAN LAACADCYVF CYPNAGLPNA MGGYDQKGDE MAEEIRPFCE GNLVNAIGGC 300 CGTGPEHIAA IKKMASAYKP RKPVTVPPLM RLSGLEPLNY TPDASNMRRT FLNIGERCNV 360 AGSILFKKAI VNNDFDTAVA IALKQVQQGA DVLDINMDDG LIEGVGAMTR FVNLLVSDPE 420 ISRVPFMIDS SKFHIVEAGL KCSQGKCIVN SISLKEGEAA FRHQAEVVRR HGAAVVVMAF 480 DEQGQAASYE EKIRICSRAY RILVEEVGFD PQDIIFDPNI LTIGTGLPEH NNYAVDFIRA 540 TREIKRLCPG SKVSGGVSNI AFSFRGNEAV RRAFHSAFLH HACLAGMDMG IVNAAQVKED 600 EYSKIDKELL EFVEDVLLNR CENATERMLE YAASLDPKSK PTAKEESWRD LPVEKRIEYA 660 LIKGIDEFAV VDTEEARSSG RYTKPLQVIE GPLMDGMNVV GDLFGAGKMF LPQVIKSARV 720 MKKAVAHLIP FIEEEKRLSG NVGENSNAGC FLIATVKGDV HDIGKNIVSV VLGCNNFKVI 780 DMGVMTPWEK ILDAAVEHKA DIIGLSGLIT PSLDEMVTVA KKMEERGMKT PLLIGGATTS 840 KMHTAVKIAP VYSGPVVHVL DASRSVPVCQ AFVDKNDKQR QVRDSYIEEV SEQYADLREE 900 FYASLEDRKY LSLADARKRA LAVDWKDPVN QPVKPKVLGN KVIRAFPIED VLDYIDWNPF 960 FQVWQLRGRY PNRGFPRIFN DATVGSEAKK LYEEAQAMLR DFVVNKRVTL NAVMGLYPAA 1020 AVGDDIEVYA DDSRAKVVAR LAGLRQQAEK DGGEPFYCIS DFVAPKGSGV PDYVGMFACS 1080 AGHGLEKVIE GYKAAGDDYS YIMAEALADR LAEALAEKLH ELVRREYWGY APDEKLSVDD 1140 MLKVKYQGIR PAPGYPSQPD HTEKRTMWEL LDAEAATDIK LTESLAMWPA ASVSGLYFGG 1200 KCSSYFAVGK ITREQVEDYA ARKKMDIKDA ERWLSTMLNY EP 1242 Gene Ontology GO:0005622; C: intracellular; IEA: InterPro GO:0031419; F: cobalamin binding; IEA: UniProtKB-KW GO:0008898; F: S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA: InterPro GO:0008705; F: methionine synthase activity; IEA: UniProtKB-EC GO:0008270; F: zinc ion binding; IEA: InterPro GO:0042558; P: pteridine-containing compound metabolic process; IEA: InterPro Interpro Pfam SMART SMART; SM01018; B12-binding_2 PROSITE PRINTS |