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P80862 (SERC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoserine aminotransferase
EC=2.6.1.52
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name=PSAT
Vegetative protein 234
Short name=VEG234
Gene names
Name:serC
Synonyms:yhaF
Ordered Locus Names:BSU10020
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Pyridoxal phosphate 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.

Caution

According to Ref.4, SerC is not involved in pyridoxine biosynthesis in B.subtilis. In this organism, pyridoxal phosphate biosynthesis is achieved via an alternative pathway involving PdxS and PdxT.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Phosphoserine aminotransferase HAMAP MF_00160
PRO_0000150153

Regions

Region76 – 772Pyridoxal phosphate binding By similarity
Region235 – 2362Pyridoxal phosphate binding By similarity

Sites

Binding site421L-glutamate By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site1511Pyridoxal phosphate By similarity
Binding site1701Pyridoxal phosphate By similarity
Binding site1931Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1941N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict51T → W AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P80862 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 29EEEF609F1EFF9D

FASTA35940,136
        10         20         30         40         50         60 
MERTTNFNAG PAALPLEVLQ KAQKEFIDFN ESGMSVMELS HRSKEYEAVH QKAKSLLIEL 

        70         80         90        100        110        120 
MGIPEDYDIL FLQGGASLQF SMLPMNFLTP EKTAHFVMTG AWSEKALAET KLFGNTSITA 

       130        140        150        160        170        180 
TSETDNYSYI PEVDLTDVKD GAYLHITSNN TIFGTQWQEF PNSPIPLVAD MSSDILSRKI 

       190        200        210        220        230        240 
DVSKFDVIYG GAQKNLGPSG VTVVIMKKSW LQNENANVPK ILKYSTHVKA DSLYNTPPTF 

       250        260        270        280        290        300 
AIYMLSLVLE WLKENGGVEA VEQRNEQKAQ VLYSCIDESN GFYKGHARKD SRSRMNVTFT 

       310        320        330        340        350 
LRDDELTKTF VQKAKDAKMI GLGGHRSVGG CRASIYNAVS LEDCEKLAAF MKKFQQENE

« Hide

References

« Hide 'large scale' references
[1]"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
Microbiology 144:859-875(1998) [PubMed: 9579061] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
Electrophoresis 18:1451-1463(1997) [PubMed: 9298659] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-11.
Strain: 168 / IS58.
[4]"serC is involved in vitamin B6 biosynthesis in Escherichia coli but not in Bacillus subtilis."
Sakai A., Kita M., Katsuragi T., Tani Y.
J. Biosci. Bioeng. 93:334-337(2002) [PubMed: 16233211] [Abstract]
Cited for: NON-INVOLVEMENT IN PYRIDOXINE BIOSYNTHESIS.
Strain: CRK6000.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y14077 Genomic DNA. Translation: CAA74411.1.
AL009126 Genomic DNA. Translation: CAB12842.1.
PIRD69705.
RefSeqNP_388883.1. NC_000964.3.

3D structure databases

ProteinModelPortalP80862.
SMRP80862. Positions 6-356.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003828; EBBACP00000003828; EBBACG00000003820.
GeneID936304.
GenomeReviewsGene locus BSU10020 in contig AL009126_GR.
KEGGbsu:BSU10020.
NMPDRfig|224308.1.peg.1002.
PATRIC18973700. VBIBacSub10457_1044.

Organism-specific databases

GenoListBSU10020. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002587.
HOGENOMHBG289982.
OMAYEVLFLQ.
PhylomeDBP80862.
ProtClustDBPRK05355.

Enzyme and pathway databases

BioCycBSUB:BSU10020-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_BACSU
AccessionPrimary (citable) accession number: P80862
Secondary accession number(s): O07514
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: January 25, 2012
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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