Q64UR4 (SERC_BACFR) Reviewed, UniProtKB/Swiss-Prot

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:	BF2018

Organism

Bacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]

Taxonomic identifier

295405 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
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. 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.

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: UniProtKB-KW 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: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
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_0000150149
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)
	Q64UR4 [UniParc]. Last modified October 25, 2004. 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]

"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation." Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y. Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YCH46.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006841 Genomic DNA. Translation: BAD48765.1.
RefSeq	YP_099299.1. NC_006347.1.
3D structure databases
ProteinModelPortal	Q64UR4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3084318.
GenomeReviews	Gene locus BF2018 in contig AP006841_GR.
KEGG	bfr:BF2018.
PATRIC	21049697. VBIBacFra17906_1962.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289982.
OMA	YEVLFLQ.
PhylomeDB	Q64UR4.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	BFRA295405:BF2018-MONOMER.
Family and domain databases
HAMAP	MF_00160. SerC_aminotrans_5. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. 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]
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.
KO	K00831.
PANTHER	PTHR21152:SF1. PTHR21152:SF1. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
PIRSF	PIRSF000525. SerC. 1 hit.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_BACFR

Accession

Primary (citable) accession number: Q64UR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program