Methionine synthase - Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667)

Preferred order of sections

Names and origin

Protein names

Submitted name:
Methionine synthase EMBL ACY21686.1
EC=2.1.1.13 EMBL ACY21686.1

Gene names

Ordered Locus Names:

Gbro_2445

Organism

Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667) (Rhodococcus bronchialis) [Complete proteome] [HAMAP] EMBL ACY21686.1

Taxonomic identifier

526226 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Gordoniaceae › Gordonia ›

Protein attributes

Sequence length	1199 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Cofactor

Binds 1 zinc ion per subunit By similarity. PIRSR PIRSR000381-1

Cobalamin By similarity. PIRSR PIRSR000381-2

Ontologies

Keywords
Ligand	Cobalamin PIRSR PIRSR000381-2 Cobalt Metal-binding PIRSR PIRSR000381-1 S-adenosyl-L-methionine PIRSR PIRSR000381-2 Zinc PIRSR PIRSR000381-1
Molecular function	Methyltransferase EMBL ACY21686.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	pteridine-containing compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: InterPro methionine synthase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

827 – 828

2

Cobalamin-binding By similarity PIRSR PIRSR000381-2

Region

1196 – 1197

2

S-adenosyl-L-methionine binding By similarity PIRSR PIRSR000381-2

Sites

Metal binding

240

1

Zinc By similarity PIRSR PIRSR000381-1

Metal binding

306

1

Zinc By similarity PIRSR PIRSR000381-1

Metal binding

307

1

Zinc By similarity PIRSR PIRSR000381-1

Metal binding

750

1

Cobalt (cobalamin axial ligand) By similarity PIRSR PIRSR000381-1

Binding site

948

1

S-adenosyl-L-methionine By similarity PIRSR PIRSR000381-2

Binding site

1142

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity PIRSR PIRSR000381-2

Binding site

1146

1

Cobalamin; via carbonyl oxygen By similarity PIRSR PIRSR000381-2

Sequences

Sequence

Length

Mass (Da)

Tools

D0LDR3 [UniParc].

Last modified December 15, 2009. Version 1.
Checksum: 4F71BBF1480F805E
Show »

FASTA

1,199

130,734

        10         20         30         40         50         60 
MSSVSRPDHS TDPADFDTTF MSAMSRRVLI GDGAMGTMLQ AADLTLDDFN GLEGCNEILN 

        70         80         90        100        110        120 
DARPDVLEGI HRAYFEAGAD AVETNTFGCN LSNLGDYDIA DRIRELAYKG TGIARGVADE 

       130        140        150        160        170        180 
MGPTANGTDR FVLGSIGPGT KLPSLGHTTF AVIRDAYFEC VAGMLDGGAD AILIETSQDL 

       190        200        210        220        230        240 
LQVKAAVVAA RRAMDKLGRR IPIISHVTVE TTGTMLLGSE IGAALTAIEP LGVDMIGLNC 

       250        260        270        280        290        300 
ATGPAEMSEH LRYLSRHARI PVSVMPNAGL PVLGPNGAEY PLSPEELAQA LHGFVAEFGL 

       310        320        330        340        350        360 
DFVGGCCGTT PEHIRQVAEA VHGATPAART PEHASETSSL YTAVPFDQDA SFLVIGERTN 

       370        380        390        400        410        420 
TNGSKAFREA MIAGDYQRCL DIAKDQTRDG AHMLDLNVDY VGRDGAVDMT ALASRFATSS 

       430        440        450        460        470        480 
TLPIMLDSTE PEVIRAGLET LGGRCAVNSV NYEDGDGPNS RFTRIMQLVV EHGAAVVALT 

       490        500        510        520        530        540 
IDEEGQARTA DWKVRIAERL IADITGNWGL AEEDIIIDAL TFPISTGQEE VRRDGIETIE 

       550        560        570        580        590        600 
AIRRIHEAHP EVHFTLGISN ISFGLNPAAR QVLNSVFLHE CVQAGLDTAI VHASKILPMA 

       610        620        630        640        650        660 
RIPEEHRKVA LDLVYDRRAP GYDPLQKLME LFEGVSAASA RESRAAELAK LPLFERLERR 

       670        680        690        700        710        720 
IVDGERNGLE DDLDEAMTTV PPLKIINETL LSGMKTVGEL FGSGQMQLPF VLQSAEVMKT 

       730        740        750        760        770        780 
AVAHLEPHME STGEDGKGRI VLATVKGDVH DIGKNLVDII LSNNGYEVVN IGIKQPITNI 

       790        800        810        820        830        840 
LDVAADKKVD VIGMSGLLVK STVVMKENLE EINARGLADE YPVLLGGAAL TRSYVENDLS 

       850        860        870        880        890        900 
ETYEGDVHYA RDAFEGLRLM DEIMATKRGE GPDPDSPEAI AAAEKAAERK ARHDRSKRIA 

       910        920        930        940        950        960 
AKRKAAEEPV EVPARSDVAA DNDIPAPPFW GTRIVKGVPV ADYLQLLDER ALFLGQWGLR 

       970        980        990       1000       1010       1020 
GARGGDGPSY EDLVESEGRP RLRYWIDRLA TEGILQHAAV VYGYFPAVSD GDTVHVLTEP 

      1030       1040       1050       1060       1070       1080 
RPDAPVRYSF GFPRQQRSRF LCIADFIRSR EDAIRDGHVD VLPFQLVTMG QPIADFANEL 

      1090       1100       1110       1120       1130       1140 
FAADAYRDYL EVHGIGVQLT EALAEYWHQR VRSELRFGER TMDSEDPDEA QGFFDLEYRG 

      1150       1160       1170       1180       1190 
ARFSFGYGAC PDLDDRAKMM ELLQPERIGV HLSEELQLHP EQSTDAFVLH HPEAKYFNT

« Hide

References

[1]

"The complete chromosome of Gordonia bronchialis DSM 43247."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.

Eisen J.A.
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25592 / DSM 43247 / JCM 3198 / NCTC 10667.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001802 Genomic DNA. Translation: ACY21686.1.
RefSeq	YP_003273579.1. NC_013441.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	526226.Gbro_2445.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACY21686; ACY21686; Gbro_2445.
GeneID	8551809.
KEGG	gbr:Gbro_2445.
PATRIC	32184503. VBIGorBro114338_2502.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1410.
HOGENOM	HOG000251408.
KO	K00548.
OMA	NGSKAFR.
Enzyme and pathway databases
BioCyc	GBRO526226:GHJF-2558-MONOMER.
Family and domain databases
Gene3D	1.10.1240.10. 1 hit. 3.10.196.10. 1 hit. 3.20.20.20. 1 hit. 3.20.20.330. 1 hit. 3.40.50.280. 1 hit.
InterPro	IPR003759. Cbl-bd_cap. IPR006158. Cobalamin-bd. IPR011005. Dihydropteroate_synth-like. IPR011822. MetH. IPR000489. Pterin-binding. IPR003726. S_MeTrfase. IPR004223. VitB12-dep_Met_synth_activ_dom. [Graphical view]
Pfam	PF02310. B12-binding. 1 hit. PF02607. B12-binding_2. 1 hit. PF02965. Met_synt_B12. 1 hit. PF00809. Pterin_bind. 1 hit. PF02574. S-methyl_trans. 1 hit. [Graphical view]
PIRSF	PIRSF000381. MetH. 1 hit.
SMART	SM01018. B12-binding_2. 1 hit. [Graphical view]
SUPFAM	SSF52242. Cbl-bd. 1 hit. SSF51717. DHP_synth_like. 1 hit. SSF56507. Met_synth_B12. 1 hit. SSF47644. Met_synth_Cbl-bd. 1 hit. SSF82282. S_methyl_trans. 1 hit.
TIGRFAMs	TIGR02082. metH. 1 hit.
PROSITE	PS50974. ADOMET_ACTIVATION. 1 hit. PS51332. B12_BINDING. 1 hit. PS51337. B12_BINDING_NTER. 1 hit. PS50970. HCY. 1 hit. PS50972. PTERIN_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

D0LDR3_GORB4

Accession

Primary (citable) accession number: D0LDR3

Entry history

Integrated into UniProtKB/TrEMBL:	December 15, 2009
Last sequence update:	December 15, 2009
Last modified:	May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information