Reviewed, UniProtKB/Swiss-Prot Q0I322 (SERC_HAES1)

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:	HS_0611

Organism

Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]

Taxonomic identifier

205914 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Histophilus

Protein attributes

Sequence length	358 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 – 358	358	Phosphoserine aminotransferase HAMAP MF_00160		PRO_1000058212
Regions
	Region	75 – 76	2	Pyridoxal phosphate binding By similarity
	Region	235 – 236	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	41	1	L-glutamate By similarity
	Binding site	101	1	Pyridoxal phosphate By similarity
	Binding site	150	1	Pyridoxal phosphate By similarity
	Binding site	170	1	Pyridoxal phosphate By similarity
	Binding site	193	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	194	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0I322-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 72D89787F0B34BC0	FASTA	358	40,032
	10 20 30 40 50 60 MQVFNFSAGP AMMPKVVLEQ AQQELLNWLD QGTSVMEVSH RGKYFMEMIT QAEKDFRQLY 70 80 90 100 110 120 NIPENYKVLF LQGGARGQFA AIPMNLANKK GKTLYLTSGH WSATAAKEAR LFTEVDEINI 130 140 150 160 170 180 LLDGKLEVGE LDFSHIASQY DYVHYCPNET ISGVEIVDVP NVGEAVLVAD MSSNILSREI 190 200 210 220 230 240 DISKFGVIYA GAQKNLGPAG ITVVIVREDL IGHARKETPS IWNYEIQSKN SSMINTPPTF 250 260 270 280 290 300 AWYLCSLVFK YLLAQGGIKE MAKLNREKAK LLYDFLDQSD FYHNVVAPKN RSLMNVTFTT 310 320 330 340 350 NNDELNAKFV AEATACGLQA LKGHKVLGGM RASIYNAMPI EGIKALIEFM RKFEAENN

References

[1]

"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd." Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J. J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000436 Genomic DNA. Translation: ABI24888.1.
RefSeq	YP_718823.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0I322.
Genome annotation databases
GeneID	4240097.
GenomeReviews	Gene locus HS_0611 in contig CP000436_GR.
KEGG	hso:HS_0611.
NMPDR	fig|205914.1.peg.1336.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0I322.
OMA	SMYNTPP.
Enzyme and pathway databases
BioCyc	HSOM205914:HS_0611-MON.
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_HAES1

Accession

Primary (citable) accession number: Q0I322

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 3, 2006
Last modified:	November 3, 2009
This is version 30 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)