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A9B6Q3 (SERC_HERA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:
Phosphoserine aminotransferase

EC=2.6.1.52
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name=PSAT
Gene names
Name:serC
Ordered Locus Names:Haur_1719
OrganismHerpetosiphon aurantiacus (strain ATCC 23779 / DSM 785) [Complete proteome] [HAMAP]
Taxonomic identifier316274 [NCBI]
Taxonomic lineageBacteriaChloroflexiHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity. HAMAP MF_00160

Catalytic activity

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP MF_00160

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP MF_00160

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_00160

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP MF_00160

Subunit structure

Homodimer By similarity. HAMAP MF_00160

Subcellular location

Cytoplasm By similarity HAMAP MF_00160.

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Phosphoserine aminotransferase HAMAP MF_00160
PRO_1000097214

Regions

Region75 – 762Pyridoxal phosphate binding By similarity
Region236 – 2372Pyridoxal phosphate binding By similarity

Sites

Binding site411L-glutamate By similarity
Binding site1011Pyridoxal phosphate By similarity
Binding site1511Pyridoxal phosphate By similarity
Binding site1711Pyridoxal phosphate By similarity
Binding site1941Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1951N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9B6Q3 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 0C74CCCEDA8CA4F6

FASTA36039,196
        10         20         30         40         50         60 
MTVYNFNAGP AILPPSVLSQ AQEELRDFAG TGISVMETSH RAKEFEAVNN EVEARFKALL 

        70         80         90        100        110        120 
GIESGYRVLL LQGGASTQFA MIPMNFLGAD QVADYIITGT WAEKARDEAQ KIGKVHIAAT 

       130        140        150        160        170        180 
TEAENHNRIP SQTELQFSEN PVYVHLTTNN TIYGTQWQST PETNGVPIVA DMSSDIFSRP 

       190        200        210        220        230        240 
FDASKFGLVY AGAQKNLGPS GVTVVLIRED WLDKGAKNVP TMLRYSTHAK NNSLYNTPPT 

       250        260        270        280        290        300 
FGVYMLNLVL AWIQEQGGLA GMAEYNTRKA NVVYNAIDNS GGFYRGHAVA DSRSQMNVTF 

       310        320        330        340        350        360 
NLPTQELEKQ FLAEAKAQGM IGLPGHRSVG GVRASIYNAM SIEGVEALAS FMAHFAAKQG 

« Hide

References

[1]"Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Bryant D.A., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23779 / DSM 785.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000875 Genomic DNA. Translation: ABX04362.1.
RefSeqYP_001544490.1. NC_009972.1.

3D structure databases

ProteinModelPortalA9B6Q3.
SMRA9B6Q3. Positions 2-360.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9B6Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5733606.
GenomeReviewsGene locus Haur_1719 in contig CP000875_GR.
KEGGhau:Haur_1719.
PATRIC22120473. VBIHerAur93466_1767.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289982.
OMAYEVLFLQ.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycHAUR316274:HAUR_1719-MONOMER.

Family and domain databases

HAMAPMF_00160. SerC_aminotrans_5.
[Tree]
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[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.
KOK00831.
PANTHERPTHR21152:SF1. PTHR21152:SF1. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000525. SerC. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01364. SerC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSERC_HERA2
AccessionPrimary (citable) accession number: A9B6Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 35 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