Reviewed, UniProtKB/Swiss-Prot Q81BC0 (SERC_BACCR)

Names and origin

Protein names

Recommended name:
    Phosphoserine aminotransferase
    EC=2.6.1.52
Alternative name(s):
    Phosphohydroxythreonine aminotransferase
      Short name=PSAT

Gene names

Name:	serC
Ordered Locus Names:	BC_3249

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.
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.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 360	360	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150145
Regions
	Region	76 – 77	2	Pyridoxal phosphate binding By similarity
	Region	237 – 238	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	42	1	L-glutamate By similarity
	Binding site	102	1	Pyridoxal phosphate By similarity
	Binding site	152	1	Pyridoxal phosphate By similarity
	Binding site	172	1	Pyridoxal phosphate By similarity
	Binding site	195	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	196	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81BC0-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B8A9FBB93E2E56F2	FASTA	360	40,499
	10 20 30 40 50 60 MERVYNFSAG PSILPLPVLE KVQKELLNYN GTGMSIMEMS HRSSYFQSII EEASNLLREL 70 80 90 100 110 120 MSIPDEYEVL FLQGGASLQF SMIPLNLMNT YKKAGYVLTG SWSKKALQEA EKVGEVQVIA 130 140 150 160 170 180 SSEQEKFTTI PKLDGLLSDE KLDYVHITTN NTIEGTKYVD IPHVEKVPLV ADMSSNILSE 190 200 210 220 230 240 RYDVSKFGLI YAGAQKNLGP AGLTIAIIKR DLIGEADRSC PTMLNYETYS KNNSLYNTPP 250 260 270 280 290 300 SFSIYVTKLV LEWLKEQGGV SAIEEQNRMK SSLLYNFLDE SKLFTSPVDP TYRSLMNIPF 310 320 330 340 350 360 TTPSEELNSE FLQKAKERGL VTLKGHRSVG GMRASIYNAM PVQGVQQLVN YMKEFELENR

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016877 Genomic DNA. Translation: AAP10190.1.
RefSeq	NP_832989.1.
3D structure databases
HSSP	HSSP built from PDB template 1BT4 based on UniProtKB Q59196.
ModBase	Search...
Protein-protein interaction databases
STRING	Q81BC0.
Genome annotation databases
GeneID	1205596.
GenomeReviews	Gene locus BC_3249 in contig AE016877_GR.
KEGG	bce:BC3249.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q81BC0.
OMA	SMYNTPP.
Enzyme and pathway databases
BioCyc	BCER226900:BC_3249-MON.
Family and domain databases
HAMAP	MF_00160. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR003248. Pser_amintransf. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
ProDom	PD001544. Pser_amintransf. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01364. serC_1. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_BACCR

Accession

Primary (citable) accession number: Q81BC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)