A9IJI3 (SERC_BORPD) 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:	Bpet1884

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	376 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 – 376	376	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000097203
Regions
	Region	253 – 254	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	42	1	L-glutamate By similarity
	Binding site	104	1	Pyridoxal phosphate By similarity
	Binding site	163	1	Pyridoxal phosphate By similarity
	Binding site	188	1	Pyridoxal phosphate By similarity
	Binding site	211	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	212	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9IJI3 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 98C8E4BBC7A13011	FASTA	376	40,688
	10 20 30 40 50 60 MARPWNFSAG PSALPEAVLQ QAADEMLDWN GSGMSVMEMS HRGKHFVQIC DQAEADLRDL 70 80 90 100 110 120 LGVPADYAVM FMQGGGLGEN AIVPMNLIGR RGHPAADFVL TGHWSTRSHK EAGRYGDIHV 130 140 150 160 170 180 AASAGEAASV DGREQAPWTW VPPADTWKVR PEAAYLHLCS NETIHGVEFT DWPDLAALGA 190 200 210 220 230 240 PDVPLVVDAS SHFLSRPMDV TRAGLLFAGA QKNAGPAGVT MVVARRDLIG KALPICPSAF 250 260 270 280 290 300 DYANVAAEHS RYNTPPAFAI YIAGLVFKWV KAQGGVAGME AANRAKAELL YGYLDSTSFY 310 320 330 340 350 360 HNPVHAPVRS RMNVPFVLRD ESLNDAFLQG AEAAGLMQLK GHKSVGGMRA SIYNAMPLEG 370 VRALVEYLRD FERRYG

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP42223.1.
RefSeq	YP_001630492.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9IJI3.
ModBase	Search...
Protein-protein interaction databases
STRING	A9IJI3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5819299.
GenomeReviews	Gene locus Bpet1884 in contig AM902716_GR.
KEGG	bpt:Bpet1884.
PATRIC	21165227. VBIBorPet31633_1878.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289982.
OMA	VPENYKV.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	BPET94624:BPET1884-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_BORPD

Accession

Primary (citable) accession number: A9IJI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
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