Reviewed, UniProtKB/Swiss-Prot Q8F930 (SERC_LEPIN)

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:	LA_0366

Organism

Leptospira interrogans [Complete proteome] [HAMAP]

Taxonomic identifier

173 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	363 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-glyceric acid: 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 – 363	363	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150182
Regions
	Region	80 – 81	2	Pyridoxal phosphate binding By similarity
	Region	241 – 242	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	46	1	L-glutamate By similarity
	Binding site	106	1	Pyridoxal phosphate By similarity
	Binding site	156	1	Pyridoxal phosphate By similarity
	Binding site	176	1	Pyridoxal phosphate By similarity
	Binding site	199	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	200	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8F930-1 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: 07747CC7A2F7A554	FASTA	363	40,587
	10 20 30 40 50 60 MYLFQERIYN FGAGPAMLPN EVMEIAAAEF LNYKGSGMSV MEVSHREPLF EDVITEAEIL 70 80 90 100 110 120 LRKLLNLGED YSIAFFSGGA TLHFSALPLN LLKEGESFDV AHTGIWTKKA WEEGLKFNEV 130 140 150 160 170 180 NVIYDSTNNH FTDVPVLTDS NLSGKGKYLH ITSNNTIYGT QYPEIPKIKQ IPLVADMTSE 190 200 210 220 230 240 LLSRKIDVKD FGVIFAGAQK NIGPSGLSLA IIRNDLLGIS GRKIPILLDY SVMVKNRSLY 250 260 270 280 290 300 NTPSTYSIYI AKLVFEWLLK LGGIEAIEKV NEQKAKLIYD FIDSSSLYVC PVQKRARSKM 310 320 330 340 350 360 NVVFLLKDKN LDSKFLDEAE KNGLHGLGGH RLVGGFRASI YNSMPLTGVQ KLVSFMKDFE SKI

References

[1]

"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing." Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P. Nature 422:888-893(2003) [PubMed: 12712204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 56601 / Serogroup Icterohaemorrhagiae / Serovar lai.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE010300 Genomic DNA. Translation: AAN47566.1. Different initiation.
RefSeq	NP_710548.2.
3D structure databases
HSSP	HSSP built from PDB template 1BJN based on UniProtKB P23721.
ModBase	Search...
Genome annotation databases
GeneID	1149710.
GenomeReviews	Gene locus LA_0366 in contig AE010300_GR.
KEGG	lil:LA0366.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8F930.
Enzyme and pathway databases
BioCyc	LINT189518:LA0367-MON.
BRENDA	2.6.1.52. 258108.
Family and domain databases
HAMAP	MF_00160. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR003248. Pser_amintransf. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 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_LEPIN

Accession

Primary (citable) accession number: Q8F930

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 10, 2007
Last modified:	June 16, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)