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F0RKC6 (F0RKC6_DEIPM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism By similarity. HAMAP-Rule MF_00051

Interconversion of serine and glycine By similarity. RuleBase RU000585

Catalytic activity

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. HAMAP-Rule MF_00051 RuleBase RU000585

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00051 RuleBase RU000585

Pathway

Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. HAMAP-Rule MF_00051

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_00051 RuleBase RU000585

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00051

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00051.

Sequence similarities

Belongs to the SHMT family. HAMAP-Rule MF_00051 RuleBase RU004104

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region122 – 1243Substrate binding By similarity HAMAP-Rule MF_00051

Sites

Binding site321Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site521Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site541Substrate By similarity HAMAP-Rule MF_00051
Binding site621Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site961Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site1181Substrate; via carbonyl oxygen By similarity HAMAP-Rule MF_00051
Binding site1731Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2011Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2261Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2331Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2591Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_00051
Binding site3591Pyridoxal phosphate By similarity HAMAP-Rule MF_00051

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00051

Sequences

Sequence LengthMass (Da)Tools
F0RKC6 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 50F1AB5C003E8F83

FASTA40543,512
        10         20         30         40         50         60 
MTTPLEQKDQ TVFDLIQQEA ERQRLGLELI ASENFTSAAV REAVGSIATN KYAEGYPGKR 

        70         80         90        100        110        120 
WYGGCEVIDK IEQLAIDRAC ELFGAAWANV QPHSGSSANI AVYAALLEEG DTVMGMDLSH 

       130        140        150        160        170        180 
GGHLTHGSPV NFSGKRFNIV GYRVDEETER LDMEAVRALA LEHRPKMIIA GASAYSRQID 

       190        200        210        220        230        240 
FAAFRAIADE VGAYLFADIA HIAGLVAAGL HPNPVPHAHI VATTTHKTLR GPRSGLLLSN 

       250        260        270        280        290        300 
DPELGAKIDR AIFPGHQGGP LEHVIAGKAV AFGEALQPAF KDYAAQIIKN AQALAAAMEA 

       310        320        330        340        350        360 
RGYRIVTGGT DNHMFLADLR PQGLNGTKAT QALDANFITI SKSTLPFDTE KILHGGGIRI 

       370        380        390        400 
GTPAVTTRGM KESDMDRVAD LIDRALKGED VKEEVHAFAG QFPMP

« Hide

References

[1]"The complete sequence of chromosome of Deinococcus proteolyticus DSM 20540."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F. expand/collapse author list , Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P., Eisen J.A.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002536 Genomic DNA. Translation: ADY26705.1.
RefSeqYP_004256322.1. NC_015161.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY26705; ADY26705; Deipr_1567.
GeneID10257062.
KEGGdpt:Deipr_1567.
PATRIC46930958. VBIDeiPro159979_1558.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00600.

Enzyme and pathway databases

UniPathwayUPA00193.
UPA00288; UER01023.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERPTHR11680. PTHR11680. 1 hit.
PfamPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF0RKC6_DEIPM
AccessionPrimary (citable) accession number: F0RKC6
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info