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Protein

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

Gene

MET6

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.

Catalytic activityi

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.

Cofactori

Zn2+By similarity

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetE route).
Proteins known to be involved in this subpathway in this organism are:
  1. 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (MET6)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetE route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi657 – 6571ZincBy similarity
Metal bindingi659 – 6591ZincBy similarity
Metal bindingi739 – 7391ZincBy similarity

GO - Molecular functioni

  • 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Source: CGD
  • zinc ion binding Source: CGD

GO - Biological processi

  • cellular response to heat Source: CGD
  • induction by symbiont of host defense response Source: CGD
  • methionine biosynthetic process Source: CGD
  • methionine metabolic process Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00051; UER00082.

Names & Taxonomyi

Protein namesi
Recommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC:2.1.1.14)
Alternative name(s):
Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme
Gene namesi
Name:MET6
ORF Names:CaO19.10083, CaO19.2551
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000186137. MET6.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: CGD
  • fungal-type cell wall Source: CGD
  • hyphal cell wall Source: CGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 7677665-methyltetrahydropteroyltriglutamate--homocysteine methyltransferasePRO_0000098702Add
BLAST

2D gel databases

COMPLUYEAST-2DPAGEP82610.

Structurei

Secondary structure

1
767
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi17 – 2610Combined sources
Beta strandi28 – 303Combined sources
Helixi32 – 5322Combined sources
Beta strandi59 – 613Combined sources
Helixi68 – 758Combined sources
Helixi81 – 844Combined sources
Helixi90 – 9910Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi128 – 1303Combined sources
Helixi144 – 1463Combined sources
Helixi149 – 15911Combined sources
Beta strandi165 – 1695Combined sources
Helixi171 – 1766Combined sources
Beta strandi178 – 1803Combined sources
Helixi182 – 1843Combined sources
Helixi189 – 1924Combined sources
Helixi193 – 21018Combined sources
Beta strandi214 – 2185Combined sources
Helixi220 – 2234Combined sources
Helixi228 – 2314Combined sources
Helixi233 – 2419Combined sources
Beta strandi248 – 2525Combined sources
Helixi259 – 2613Combined sources
Helixi262 – 2654Combined sources
Beta strandi271 – 2766Combined sources
Turni277 – 2793Combined sources
Helixi281 – 2833Combined sources
Helixi284 – 2896Combined sources
Beta strandi296 – 3027Combined sources
Helixi312 – 32615Combined sources
Helixi328 – 3303Combined sources
Beta strandi331 – 3377Combined sources
Helixi339 – 3413Combined sources
Helixi346 – 3483Combined sources
Beta strandi350 – 3523Combined sources
Helixi354 – 3574Combined sources
Helixi363 – 37715Combined sources
Helixi383 – 39816Combined sources
Turni400 – 4023Combined sources
Helixi405 – 4128Combined sources
Helixi417 – 4193Combined sources
Helixi425 – 43612Combined sources
Helixi453 – 46311Combined sources
Helixi469 – 48921Combined sources
Beta strandi493 – 4953Combined sources
Helixi507 – 5104Combined sources
Beta strandi513 – 5175Combined sources
Beta strandi524 – 5274Combined sources
Beta strandi530 – 5323Combined sources
Beta strandi536 – 5427Combined sources
Helixi549 – 5579Combined sources
Beta strandi563 – 5686Combined sources
Helixi570 – 5756Combined sources
Beta strandi581 – 5833Combined sources
Helixi585 – 60521Combined sources
Beta strandi610 – 6145Combined sources
Helixi618 – 6214Combined sources
Beta strandi624 – 6274Combined sources
Helixi628 – 64518Combined sources
Beta strandi646 – 6483Combined sources
Beta strandi652 – 6587Combined sources
Beta strandi660 – 6623Combined sources
Helixi665 – 6717Combined sources
Beta strandi674 – 6785Combined sources
Beta strandi682 – 6843Combined sources
Helixi686 – 6905Combined sources
Turni691 – 6944Combined sources
Beta strandi697 – 7015Combined sources
Beta strandi706 – 7083Combined sources
Helixi714 – 72512Combined sources
Helixi730 – 7323Combined sources
Beta strandi733 – 7353Combined sources
Turni740 – 7434Combined sources
Helixi746 – 76621Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PPCX-ray2.20A/B1-767[»]
3PPFX-ray2.30A1-767[»]
3PPGX-ray1.98A1-767[»]
3PPHX-ray2.80A/B1-767[»]
4L5ZX-ray2.18A1-767[»]
4L61X-ray2.13A1-767[»]
4L64X-ray2.18A1-767[»]
4L65X-ray2.31A1-767[»]
4L6HX-ray1.75A1-767[»]
4L6OX-ray1.88A1-767[»]
4QQUX-ray2.98A1-767[»]
ProteinModelPortaliP82610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82610.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP82610.
KOiK00549.
OrthoDBiEOG7BGHV7.

Family and domain databases

HAMAPiMF_00172. Meth_synth.
InterProiIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Met_Synth_C/arc.
[Graphical view]
PfamiPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsiTIGR01371. met_syn_B12ind. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P82610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQSSVLGFP RIGGQRELKK ITEAYWSGKA TVEELLAKGK ELREHNWKLQ
60 70 80 90 100
QKAGVDIIPS NDFSYYDQVL DLSLLFNAIP ERYTKFDLAP IDVLFAMGRG
110 120 130 140 150
LQKKATETQA AVDVTALEMV KWFDSNYHYV RPTFSHSTEF KLNTAAGIKP
160 170 180 190 200
VDEFNEAKAL GVQTRPVILG PVSYLYLGKA DKDSLDLEPI SLLPKILPVY
210 220 230 240 250
KELLQKLKEA GAEQVQIDEP VLVLDLPEAV QSKFKEAYDA LVGADVPELI
260 270 280 290 300
LTTYFGDVRP NLKAIENLPV AGFHFDFVRV PEQLDEVASI LKDGQTLSAG
310 320 330 340 350
VVDGRNIWKT DFAKASAVVQ KAIEKVGKDK VVVATSSSLL HTPVDLESET
360 370 380 390 400
KLDAVIKDWF SFATQKLDEV VVIAKNVSGE DVSKQLEANA ASIKARSESS
410 420 430 440 450
ITNDPKVQER LTTINEALAT RKAAFPERLT EQKAKYNLPL FPTTTIGSFP
460 470 480 490 500
QTKDIRINRN KFAKGQITAE EYEAFINKEI ETVVRFQEEI GLDVLVHGEP
510 520 530 540 550
ERNDMVQYFG EQLNGFAFTT NGWVQSYGSR YVRPPIIVGD VSRPKAMTVK
560 570 580 590 600
ESVYAQSITS KPMKGMLTGP VTILRWSFPR DDVSGKIQAL QLGLALRDEV
610 620 630 640 650
NDLEGAGITV IQVDEPAIRE GLPLRAGKER SDYLNWAAQS FRVATSGVEN
660 670 680 690 700
STQIHSHFCY SDLDPNHIKA LDADVVSIEF SKKDDPNYIQ EFSEYPNHIG
710 720 730 740 750
LGLFDIHSPR IPSKQEFVSR IEEILKVYPA SKFWVNPDCG LKTRGWPEVK
760
ESLTNMVEAA KEFRAKY
Length:767
Mass (Da):85,702
Last modified:March 3, 2009 - v2
Checksum:i21BE228C99259471
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51S → D AA sequence (PubMed:11681208).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000043 Genomic DNA. Translation: EAK99386.1.
AACQ01000044 Genomic DNA. Translation: EAK99287.1.
RefSeqiXP_718219.1. XM_713126.1.
XP_718315.1. XM_713222.1.

Genome annotation databases

EnsemblFungiiEAK99287; EAK99287; CaO19.2551.
EAK99386; EAK99386; CaO19.10083.
GeneIDi3640000.
3640084.
KEGGical:CaO19.10083.
cal:CaO19.2551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000043 Genomic DNA. Translation: EAK99386.1.
AACQ01000044 Genomic DNA. Translation: EAK99287.1.
RefSeqiXP_718219.1. XM_713126.1.
XP_718315.1. XM_713222.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PPCX-ray2.20A/B1-767[»]
3PPFX-ray2.30A1-767[»]
3PPGX-ray1.98A1-767[»]
3PPHX-ray2.80A/B1-767[»]
4L5ZX-ray2.18A1-767[»]
4L61X-ray2.13A1-767[»]
4L64X-ray2.18A1-767[»]
4L65X-ray2.31A1-767[»]
4L6HX-ray1.75A1-767[»]
4L6OX-ray1.88A1-767[»]
4QQUX-ray2.98A1-767[»]
ProteinModelPortaliP82610.
ModBaseiSearch...
MobiDBiSearch...

2D gel databases

COMPLUYEAST-2DPAGEP82610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAK99287; EAK99287; CaO19.2551.
EAK99386; EAK99386; CaO19.10083.
GeneIDi3640000.
3640084.
KEGGical:CaO19.10083.
cal:CaO19.2551.

Organism-specific databases

CGDiCAL0000186137. MET6.

Phylogenomic databases

InParanoidiP82610.
KOiK00549.
OrthoDBiEOG7BGHV7.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00082.

Miscellaneous databases

EvolutionaryTraceiP82610.

Family and domain databases

HAMAPiMF_00172. Meth_synth.
InterProiIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Met_Synth_C/arc.
[Graphical view]
PfamiPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsiTIGR01371. met_syn_B12ind. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.
  2. "Analysis of the serologic response to systemic Candida albicans infection in a murine model."
    Pitarch A., Diez-Orejas R., Molero G., Pardo M., Sanchez M., Gil C., Nombela C.
    Proteomics 1:550-559(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15.
    Strain: SC5314 / ATCC MYA-2876.
  3. "Cross-species identification of novel Candida albicans immunogenic proteins by combination of two-dimensional polyacrylamide gel electrophoresis and mass spectrometry."
    Pardo M., Ward M., Pitarch A., Sanchez M., Nombela C., Blackstock W., Gil C.
    Electrophoresis 21:2651-2659(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 411-421, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: SC5314 / ATCC MYA-2876.

Entry informationi

Entry nameiMETE_CANAL
AccessioniPrimary (citable) accession number: P82610
Secondary accession number(s): Q5A9B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 3, 2009
Last modified: February 17, 2016
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.