Reviewed, UniProtKB/Swiss-Prot A9A0A5 (SERC_DESOH)

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:	Dole_3221

Organism

Desulfococcus oleovorans (strain DSM 6200 / Hxd3) [Complete proteome] [HAMAP]

Taxonomic identifier

96561 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfobacterales › Desulfobacteraceae › Desulfococcus

Protein attributes

Sequence length	361 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: 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 – 361	361	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000097213
Regions
	Region	77 – 78	2	Pyridoxal phosphate binding By similarity
	Region	237 – 238	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	43	1	L-glutamate By similarity
	Binding site	103	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)
	A9A0A5-1 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 3B94FD99417DBB95	FASTA	361	39,461
	10 20 30 40 50 60 MSKRIYNFNP GPAALPLSVL EEIQATFLDF AGTGMSITEV SHRSKPFDAI INDAVTRVKR 70 80 90 100 110 120 LLGIGDDFKV LFVQGGASMQ FAMVPMNLLP DGKSADYVNT GTWSTKAIKE TKILGKTVNV 130 140 150 160 170 180 AASSEDRNFA YIPKELSLDP NAAYVHITSN NTIKGTQWAD FPDTKGVPIV SDMSSDILSR 190 200 210 220 230 240 PLDMSKFGLI YAGAQKNIGP AGVCMVIVKN DLLEKANTGL PSMLAYKTYA DSNSLYNTPP 250 260 270 280 290 300 CFTIYAIDLV LKWLEETIGG LEKMDAVNRE KAALLYDLFD ASSFYNGTAD ADSRSLMNVT 310 320 330 340 350 360 FRLPSEDLEK RFVEEATKND LGGLKGHRSV GGCRASIYNA MSMEGIQALV DFMKEFERTN G

References

[1]

"Complete sequence of Desulfococcus oleovorans Hxd3." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Wawrik B., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000859 Genomic DNA. Translation: ABW69024.1.
RefSeq	YP_001531101.1.
3D structure databases
SMR	A9A0A5. Positions 2-361.
ModBase	Search...
Genome annotation databases
GeneID	5696083.
GenomeReviews	Gene locus Dole_3221 in contig CP000859_GR.
KEGG	dol:Dole_3221.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289982.
OMA	TFAWYLA.
Family and domain databases
HAMAP	MF_00160. SerC_aminotrans_5. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR003248. Pser_amintransf. 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.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01364. serC_1. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_DESOH

Accession

Primary (citable) accession number: A9A0A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	January 15, 2008
Last modified:	February 9, 2010
This is version 23 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)