Reviewed, UniProtKB/Swiss-Prot A7H543 (SERC_CAMJD)

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:	JJD26997_1632

Organism

Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP]

Taxonomic identifier

360109 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	358 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 – 358	358	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000058207
Regions
	Region	75 – 76	2	Pyridoxal phosphate binding By similarity
	Region	233 – 234	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	41	1	L-glutamate By similarity
	Binding site	100	1	Pyridoxal phosphate By similarity
	Binding site	148	1	Pyridoxal phosphate By similarity
	Binding site	167	1	Pyridoxal phosphate By similarity
	Binding site	190	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	191	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7H543-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: B8699D0BD0E9082A	FASTA	358	40,470
	10 20 30 40 50 60 MRKINFSAGP STLPLEILEQ AQKEFCDYQG KGYSIMEISH RTKVFEEVHF GAQEKAKKLY 70 80 90 100 110 120 GLNDDYEVLF LQGGASLQFA MIPMNLALNG VCEYVNTGVW TKKAIKEAQI LGVNVKIVVS 130 140 150 160 170 180 SEESNFDHIP RVEFSDNADY AYICSNNTIY GTQYQNYPKT KAPLIVDASS DFFSRKVDFS 190 200 210 220 230 240 NIALFYGGVQ KNAGISGLSC IFIRKDMLER SKNKQIPSML NYLTHAENQS LFNTPPTFAI 250 260 270 280 290 300 YMFNLEMDWL LNQGGLDKVH EKNSQKATML YKCIDLSDGF YKGHADKKDR SLMNVSFNIA 310 320 330 340 350 KNKDLEPLFV KEAEEAGMIG LKGHRILGGI RASIYNALNL DQVKILCEFM KEFQGKYA

References

[1]

"Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood." Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000768 Genomic DNA. Translation: ABS43644.1.
RefSeq	YP_001398623.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7H543.
Genome annotation databases
GeneID	5389749.
GenomeReviews	Gene locus JJD26997_1632 in contig CP000768_GR.
KEGG	cjd:JJD26997_1632.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	SMYNTPP.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_CAMJD

Accession

Primary (citable) accession number: A7H543

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 11, 2007
Last modified:	November 3, 2009
This is version 19 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)