Reviewed, UniProtKB/Swiss-Prot Q7VLP0 (SERC_HAEDU)

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:	HD_1382

Organism

Haemophilus ducreyi [Complete proteome] [HAMAP]

Taxonomic identifier

730 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	362 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 – 362	362	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150173
Regions
	Region	239 – 240	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	154	1	Pyridoxal phosphate By similarity
	Binding site	174	1	Pyridoxal phosphate By similarity
	Binding site	197	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	198	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VLP0-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: C94D4B5250815E37	FASTA	362	40,112
	10 20 30 40 50 60 MKHVYNFSAG PAMMPKAVLA QAQQELLNWQ QQGTSVMEVS HRSNAFMALA TQTEQDLRQL 70 80 90 100 110 120 YAIPDNYKVL FLQGGAHGQF AAIPMNLIGK KGKALYLISG HWSNRSAQEA RNFCEVDQLN 130 140 150 160 170 180 ILTQDEAGVF SVNQTDFSDI AEQYDYVHYC PNETISGVEI PDIPIVGKAV LVADMSSNIL 190 200 210 220 230 240 SRNIDISKFG LIYAGAQKNL GPAGITIVII RQDLIGNAQR ATPSIWNYAT QVNADSMINT 250 260 270 280 290 300 PPTFAWYLCS LVFKHLRAAG GLASVEQRNQ QKAALLYQYL DNSHFYHNYV APQNRSLMNV 310 320 330 340 350 360 TFTTNNDELN AKFVAEAAEN GLHALKGHKV VGGMRASIYN AMPLDGVEAL IEFMQKFAQE NR

References

[1]

"The complete genome sequence of Haemophilus ducreyi." Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017143 Genomic DNA. Translation: AAP96195.1.
RefSeq	NP_873806.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1491274.
GenomeReviews	Gene locus HD_1382 in contig AE017143_GR.
KEGG	hdu:HD1382.
NMPDR	fig|233412.1.peg.1171.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7VLP0.
OMA	SMYNTPP.
Enzyme and pathway databases
BioCyc	HDUC233412:HD_1382-MON.
BRENDA	2.6.1.52. 265031.
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_HAEDU

Accession

Primary (citable) accession number: Q7VLP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 49 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)