A1VY45 (SERC_CAMJJ) 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:	CJJ81176_0348

Organism

Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]

Taxonomic identifier

354242 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	358 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 – 358	358	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000058208
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)
	A1VY45 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: D77A76B8B23473A2	FASTA	358	40,466
	10 20 30 40 50 60 MRKINFSAGP STLPLEILEQ AQKELCDYQG RGYSIMEISH RTKVFEEVHF GAQEKAKKLY 70 80 90 100 110 120 GLNDDYEVLF LQGGASLQFA MIPMNLALNG VCEYANTGVW TKKAIKEAQI LGVNVKTVAS 130 140 150 160 170 180 SEESNFNHIP RVEFRDNADY AYICSNNTIY GTQYQNYPKT KTPLIVDASS DFFSRKVDFS 190 200 210 220 230 240 NIALFYGGVQ KNAGISGLSC IFIRKDMLER SKNKQIPSML NYLTHAENQS LFNTPPTFAI 250 260 270 280 290 300 YMFNLEMDWL LNQGGLDKVH EKNSQKAAML YECIDLSNGF YKGHADKKDR SLMNVSFNIA 310 320 330 340 350 KNKDLEPLFV KEAEEAGMIG LKGHRILGGI RASIYNALNL DQIKTLCEFM KEFQGKYA

References

[1]	Fouts D.E., Nelson K.E., Sebastian Y. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 81-176.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000538 Genomic DNA. Translation: EAQ72981.1.
RefSeq	YP_001000036.1. NC_008787.1.
3D structure databases
ProteinModelPortal	A1VY45.
ModBase	Search...
Protein-protein interaction databases
STRING	A1VY45.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4683215.
GenomeReviews	Gene locus CJJ81176_0348 in contig CP000538_GR.
KEGG	cjj:CJJ81176_0348.
PATRIC	20050652. VBICamJej103413_0369.
TIGR	CJJ81176_0348.
Phylogenomic databases
eggNOG	COG1932.
HOGENOM	HBG289982.
OMA	YEVLFLQ.
PhylomeDB	A1VY45.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	CJEJ354242:CJJ81176_0348-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.
TIGRFAMs	TIGR01364. SerC_1. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_CAMJJ

Accession

Primary (citable) accession number: A1VY45

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 6, 2007
Last modified:	December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program