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F0SSA1 (F0SSA1_PLABD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 16. Feed History...

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

Protein namesRecommended name:
Phosphoserine aminotransferase HAMAP-Rule MF_00160 RuleBase RU004505
EC=2.6.1.52 HAMAP-Rule MF_00160 RuleBase RU004505
Alternative name(s):
Phosphohydroxythreonine aminotransferase HAMAP-Rule MF_00160
Gene names
Name:serC HAMAP-Rule MF_00160
Ordered Locus Names:Plabr_0485
OrganismPlanctomyces brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448) [Complete proteome] [HAMAP] EMBL ADY58112.1
Taxonomic identifier756272 [NCBI]
Taxonomic lineageBacteria › Planctomycetes › Planctomycetia › Planctomycetales › Planctomycetaceae › Planctomyces ›

Protein attributes

Sequence length359 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-Rule MF_00160 SAAS SAAS020578

Catalytic activity

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP-Rule MF_00160 SAAS SAAS020578

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP-Rule MF_00160 RuleBase RU004505 SAAS SAAS020578

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP-Rule MF_00160 SAAS SAAS020578

Pyridoxal phosphate By similarity. RuleBase RU004504

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP-Rule MF_00160 RuleBase RU004505 SAAS SAAS020578

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00160 SAAS SAAS020578

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00160.

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. HAMAP-Rule MF_00160

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region76 – 772Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00160
Region236 – 2372Pyridoxal phosphate binding By similarity HAMAP-Rule MF_00160

Sites

Binding site421L-glutamate By similarity HAMAP-Rule MF_00160
Binding site1021Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1501Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1711Pyridoxal phosphate By similarity HAMAP-Rule MF_00160
Binding site1941Pyridoxal phosphate By similarity HAMAP-Rule MF_00160

Amino acid modifications

Modified residue1951N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00160

Sequences

Sequence LengthMass (Da)Tools
F0SSA1 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: D75B7F7637217EC7

FASTA35938,799
        10         20         30         40         50         60 
MNRVYNFSAG PAVMPVEVLE EARENMLSLG DTGIGVMEHS HRGKPFVAVA EQAEANCRKL 

        70         80         90        100        110        120 
ANISDDYAVL FLQGGASTQF FTVPQNLLSK DKTADYLVTG SWSKKAVKEA KLFGNVNVAC 

       130        140        150        160        170        180 
SSEDRNFCYI PKECSYSDAP AYVHFTSNNT IFGTQFATEP NGPAGAPLVC DASSDIFSRP 

       190        200        210        220        230        240 
IDVSKYGIIY AGAQKNLGPS GVTLVIIRKD LIEQGPSDLP SMLQYRTHAN NDSMFNTPPT 

       250        260        270        280        290        300 
FGIFTMGLVF KWIEKQGGLA GVAQKNAAKA KPLYDYLDGS SLFKATADQD SRSLMNVCFV 

       310        320        330        340        350 
TGDADKDAKF IASAKEEGFD GLKGHRSVGG MRASIYNAFP AEGVTALVDF MRDFEAKNG

« Hide

References

[1]"The complete genome of Planctomyces brasiliensis DSM 5305."
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M., Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F. expand/collapse author list , Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., 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 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002546 Genomic DNA. Translation: ADY58112.1.
RefSeqYP_004268134.1. NC_015174.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY58112; ADY58112; Plabr_0485.
GeneID10237871.
KEGGpbs:Plabr_0485.
PATRIC47009761. VBIPlaBra152897_0529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00831.

Enzyme and pathway databases

BioCycPBRA756272:GH5Q-493-MONOMER.
UniPathwayUPA00135; UER00197.
UPA00244; UER00311.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00160. SerC_aminotrans_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
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 nameF0SSA1_PLABD
AccessionPrimary (citable) accession number: F0SSA1
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 1, 2013
This is version 16 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