A9NC17 (SERC_COXBR) 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:	COXBURSA331_A0639

Organism

Coxiella burnetii (strain RSA 331 / Henzerling II) [Complete proteome] [HAMAP]

Taxonomic identifier

360115 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

Protein attributes

Sequence length	360 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 – 360	360	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000076905
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)
	A9NC17 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: F1E36AD2C4A066E8	FASTA	360	40,631
	10 20 30 40 50 60 MSRVYNFSAG PAAIPEEVLF TVRDELLDWH GIGMSIAEVS HRGEEFIGVA EEAARDLREL 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]	"Genome sequencing of phylogenetically and phenotypically diverse Coxiella burnetii isolates." Seshadri R., Samuel J.E. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 331 / Henzerling II.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000890 Genomic DNA. Translation: ABX78179.1.
RefSeq	YP_001596457.1. NC_010117.1.
3D structure databases
ProteinModelPortal	A9NC17.
SMR	A9NC17. Positions 3-360.
ModBase	Search...
Protein-protein interaction databases
STRING	A9NC17.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5794091.
GenomeReviews	Gene locus serC in contig CP000890_GR.
KEGG	cbs:COXBURSA331_A0639.
PATRIC	17925537. VBICoxBur33747_0659.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289982.
OMA	YEVLFLQ.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	CBUR360115:COXBURSA331_A0639-MONOMER.
Family and domain databases
HAMAP	MF_00160. SerC_aminotrans_5. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_COXBR

Accession

Primary (citable) accession number: A9NC17

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program