Reviewed, UniProtKB/Swiss-Prot Q5LDN9 (SERC_BACFN)

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:	BF2072

Organism

Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]

Taxonomic identifier

272559 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	355 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 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.
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 Pyridoxine 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 pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – 355	355	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150148
Regions
	Region	75 – 76	2	Pyridoxal phosphate binding By similarity
	Region	231 – 232	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	41	1	L-glutamate By similarity
	Binding site	99	1	Pyridoxal phosphate By similarity
	Binding site	147	1	Pyridoxal phosphate By similarity
	Binding site	166	1	Pyridoxal phosphate By similarity
	Binding site	189	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	190	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LDN9-1 [UniParc]. Last modified June 21, 2005. Version 1. Checksum: 075E7241CDD4229E	FASTA	355	39,196
	10 20 30 40 50 60 MKKHNFSAGP SILPREVIEE TAKAILDFNG SGLSVLEVSH RGKDFQAVMD EAVALFKEIL 70 80 90 100 110 120 NIPEGYSVLF LGGGASMQFC MVPYNFLEKK AAYLNTGVWA KKAMKEAKGF GEVVEVASSA 130 140 150 160 170 180 DANYTFIPKD FTIPADADYF HVTTNNTIYG TELKGDLDSP VPMVADMSSD IFSRPVDVSK 190 200 210 220 230 240 YICIYGGAQK NLAPSGVTFV IVKDDAVGKV SRYIPSMLNY KTHIDGGSMF NTPPVLPIYS 250 260 270 280 290 300 AMQTLRWIKA QGGVKEMDRR ATEKADMLYA EIDRNKMFVG TAAKEDRSRM NICFVMAPEY 310 320 330 340 350 KDLEADFLKF ATDKGMSGIK GHRSVGGFRA SCYNAMPKES VQALIDCMQE FEKLH

References

[1]

"Extensive DNA inversions in the B. fragilis genome control variable gene expression." Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A. , Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J. Science 307:1463-1465(2005) [PubMed: 15746427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR626927 Genomic DNA. Translation: CAH07769.1.
RefSeq	YP_211700.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5LDN9.
Genome annotation databases
GeneID	3287528.
GenomeReviews	Gene locus BF2072 in contig CR626927_GR.
KEGG	bfs:BF2072.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5LDN9.
OMA	SMYNTPP.
Enzyme and pathway databases
BioCyc	BFRA272559:BF2072-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. 2 hits. [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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_BACFN

Accession

Primary (citable) accession number: Q5LDN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	June 21, 2005
Last modified:	November 3, 2009
This is version 38 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)