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Q11NZ7 (GLYA_CYTH3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyridoxal-phosphate-dependent serine hydroxymethyltransferase

Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:CHU_3633
OrganismCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]
Taxonomic identifier269798 [NCBI]
Taxonomic lineageBacteriaBacteroidetesCytophagiaCytophagalesCytophagaceaeCytophaga

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate serving as the one-carbon carrier By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_00051

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_00051

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00051.

Sequence similarities

Belongs to the SHMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000369916

Regions

Region125 – 1273Substrate binding By similarity

Sites

Binding site351Pyridoxal phosphate By similarity
Binding site551Pyridoxal phosphate By similarity
Binding site571Substrate By similarity
Binding site641Substrate binding By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site1211Substrate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2771Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3771Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11NZ7 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: E2309B2FEBA0D42B

FASTA43147,153
        10         20         30         40         50         60 
MITAPIRTTA RDTQIFDLIS KEAHRQEEGI ELIASENFTS KQVMEAMGSV LTNKYAEGLP 

        70         80         90        100        110        120 
GKRYYGGCQV VDQVEQIAID RLKKLFGAEW ANVQPHSGAQ ANAAIMIACL NPGDSILGFD 

       130        140        150        160        170        180 
LSHGGHLSHG SPVNMSGKYF KAHFYGVEKE SGLINMDIVE ATALKVKPKM IICGASAYSR 

       190        200        210        220        230        240 
DWDYARFRKI ADSVGAILLA DISHPAGLIA KGLLNDPIPH CHIVSTTTHK TLRGPRGGVI 

       250        260        270        280        290        300 
MMGKDFENPF GLKTPKGETR MMSNVLDMGV FPGTQGGPLE HVIAAKAVAF QEALSTDYLQ 

       310        320        330        340        350        360 
YAKQIQKNAQ IMAEAFLKKG YDIISGGTDN HLMLIDLRSK NLTGKEAENA LIRADITINK 

       370        380        390        400        410        420 
NMVPFDDKSP FVTSGMRVGT AAITSRGMVG DDMIRIVEMI DTVLMNQTKD SVIETVRKDV 

       430 
NNWMAQYPLY I 

« Hide

References

[1]"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii."
Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J.
Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed: 17400776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33406 / NCIMB 9469.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000383 Genomic DNA. Translation: ABG60866.1.
RefSeqYP_680209.1. NC_008255.1.

3D structure databases

ProteinModelPortalQ11NZ7.
SMRQ11NZ7. Positions 9-431.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ11NZ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4184877.
GenomeReviewsGene locus CHU_3633 in contig CP000383_GR.
KEGGchu:CHU_3633.
NMPDRfig|269798.12.peg.3461.
PATRIC21598145. VBICytHut34013_3617.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAFPMYADR.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycCHUT269798:CHU_3633-MONOMER.

Family and domain databases

HAMAPMF_00051. SHMT.
[Tree]
InterProIPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00600.
PANTHERPTHR11680. Gly_HO-Metrfase. 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 nameGLYA_CYTH3
AccessionPrimary (citable) accession number: Q11NZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families