Reviewed, UniProtKB/Swiss-Prot Q83E12 (SERC_COXBU)

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:	CBU_0525

Organism

Coxiella burnetii [Complete proteome] [HAMAP]

Taxonomic identifier

777 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	360 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 – 360	360	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150165
Regions
	Region	237 – 238	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	42	1	L-glutamate By similarity
	Binding site	102	1	Pyridoxal phosphate By similarity
	Binding site	152	1	Pyridoxal phosphate By similarity
	Binding site	171	1	Pyridoxal phosphate By similarity
	Binding site	194	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	195	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83E12-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A1E1A9CF69176337	FASTA	360	40,689
	10 20 30 40 50 60 MSRVYNFSAG PAAIPEEVLF TVRDELLDWH GIGMSIAEVS HRGEEFIGVA EEAERDLREL 70 80 90 100 110 120 LAVPESYHIL FLQGGSRLQF DMVPMNLLAN HKKAVYIDSG VWSNLAIREA KNYCDPHLAT 130 140 150 160 170 180 NAKELNYTGI PDQATWDMPN EAAYFYYVDN ETVNGIEFPF IPDTDLTLVC DMSSNLLSRP 190 200 210 220 230 240 FDVSRYGLIF ACAQKNMGLA GLTIVIVHDD LLKRSPLPTT PSYLQYALHA KERSFINTPP 250 260 270 280 290 300 TFAWYLAGLI FKWVKNQGGV AVLAERNQRK AAKLYKFIDK SNFFDNPINP TYRSRMNVIF 310 320 330 340 350 360 RLADERLNSL FLKEATENGL ANLKGHRLLG GMRASIYNAM TEEGVDALIN FMGQFEKRHG

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016828 Genomic DNA. Translation: AAO90071.1.
RefSeq	NP_819557.1.
3D structure databases
HSSP	HSSP built from PDB template 1BJO based on UniProtKB P23721.
ModBase	Search...
Genome annotation databases
GeneID	1208410.
GenomeReviews	Gene locus CBU_0525 in contig AE016828_GR.
KEGG	cbu:CBU_0525.
NMPDR	fig|227377.1.peg.501.
TIGR	CBU_0525.
Phylogenomic databases
HOGENOM	Q83E12.
OMA	SMYNTPP.
Enzyme and pathway databases
BioCyc	CBUR227377:CBU_0525-MON.
BRENDA	2.6.1.52. 256353.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_COXBU

Accession

Primary (citable) accession number: Q83E12

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 52 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)