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A6VP23 (GLYA_ACTSZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:Asuc_1360
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length422 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 – 422422Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000071128

Regions

Region124 – 1263Substrate binding By similarity

Sites

Binding site341Pyridoxal phosphate By similarity
Binding site541Pyridoxal phosphate By similarity
Binding site561Substrate By similarity
Binding site631Substrate binding By similarity
Binding site641Pyridoxal phosphate By similarity
Binding site981Pyridoxal phosphate By similarity
Binding site1201Substrate By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2271Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2621Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3621Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VP23 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: F348DAB2F9516A3B

FASTA42245,594
        10         20         30         40         50         60 
MLEKKTIAEL DPVLWDAMQN EVRRQEEHIE LIASENYVTP AVMQAQGSQL TNKYAEGYPG 

        70         80         90        100        110        120 
KRYYGGCEYV DIVEQLAIDR AKELFGAEYA NVQPHSGSQA NAAVYGALLS AGDTILGMDL 

       130        140        150        160        170        180 
AHGGHLTHGA KVSFSGKIYN SVLYGITADG VIDYADVRTK ALESKPKMIV AGFSAYSQVI 

       190        200        210        220        230        240 
DWAKMREIAD EVDAYLFVDM AHVAGLIAAG LYPNPLPHAH VVTTTTHKTL AGPRGGLILS 

       250        260        270        280        290        300 
ACGDEDIYKK LNSSVFPANQ GGPLMHVIAA KAVCFKEALE PSFKVYQAQV LKNAKAMVEV 

       310        320        330        340        350        360 
FKQRGFDVVS NGTENHLFLV SFIKQGLTGK QADAALGAAN ITVNKNSVPN DPQKPFVTSG 

       370        380        390        400        410        420 
IRVGSPSITR RGFSETDAAT LAGWMCDVLE SIGKDNHEQV IAETKTKVLD ICKRLPVYGI 


GR

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References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55618 / 130Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000746 Genomic DNA. Translation: ABR74720.1.
RefSeqYP_001344655.1. NC_009655.1.

3D structure databases

ProteinModelPortalA6VP23.
SMRA6VP23. Positions 1-419.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6VP23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5348520.
GenomeReviewsGene locus Asuc_1360 in contig CP000746_GR.
KEGGasu:Asuc_1360.
PATRIC20761092. VBIActSuc117883_1423.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMATECKELA.
ProtClustDBPRK00011.

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_ACTSZ
AccessionPrimary (citable) accession number: A6VP23
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 33 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

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