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A8MGL7 (GLYA_ALKOO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:Clos_1700
OrganismAlkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]
Taxonomic identifier350688 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Alkaliphilus

Protein attributes

Sequence length410 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 – 410410Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000057363

Regions

Region123 – 1253Substrate binding By similarity

Sites

Binding site331Pyridoxal phosphate By similarity
Binding site531Pyridoxal phosphate By similarity
Binding site551Substrate By similarity
Binding site621Substrate binding By similarity
Binding site631Pyridoxal phosphate By similarity
Binding site1191Substrate By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2271Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2591Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3591Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8MGL7 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 67BD4418C3248AD1

FASTA41045,240
        10         20         30         40         50         60 
MNFDTLKIAD PEIYEVIQKE TKRQRGNIEL IASENFVTEA VMEAMGSQLT NKYAEGYPGK 

        70         80         90        100        110        120 
RYYGGCEEVD VAEDLARDRL KKLFNAEHAN VQPHSGANAN IGVYFAILKP GDTVLGMNLS 

       130        140        150        160        170        180 
HGGHLTHGSP VNISGTYYNF VDYGVDKETH LINYEEVRRI ANEIKPKLIV AGASAFPRKI 

       190        200        210        220        230        240 
DFKKFREIAD EVGAYLMVDM AHIAGLVAAG LHENPCDYAD FVTTTTHKTL RGPRGGAILC 

       250        260        270        280        290        300 
KEKYAKMIDK AIFPGLQGGP LMHVIAAKAV SFKEALSPEF KAYQEQVIKN AAKLGEELKS 

       310        320        330        340        350        360 
RGFNLVSGGT DNHLLLLDLR NKNITGKDAE KLLDEVGVTV NKNTIPYDPE SPFVTSGIRI 

       370        380        390        400        410 
GTPAVTTRGM KEDDMVTIAE IIGTIIDHPE RIDEVSSMVK NLCEKFKLYE

« Hide

References

[1]"Complete genome of Alkaliphilus oremlandii OhILAs."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OhILAs.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000853 Genomic DNA. Translation: ABW19240.1.
RefSeqYP_001513236.1. NC_009922.1.

3D structure databases

ProteinModelPortalA8MGL7.
SMRA8MGL7. Positions 10-386.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8MGL7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5678469.
GenomeReviewsGene locus Clos_1700 in contig CP000853_GR.
KEGGaoe:Clos_1700.
PATRIC20868648. VBIAlkOre124042_1780.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAFSASYEM.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycAORE350688:CLOS_1700-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_ALKOO
AccessionPrimary (citable) accession number: A8MGL7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 30 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents