Q5QZ48 (SERC_IDILO) 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:	IL1359

Organism

Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]

Taxonomic identifier

283942 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length	361 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 – 361	361	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150175
Regions
	Region	76 – 77	2	Pyridoxal phosphate binding By similarity
	Region	238 – 239	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	173	1	Pyridoxal phosphate By similarity
	Binding site	196	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	197	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5QZ48 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 66AC5ACD02EC8DEC	FASTA	361	39,967
	10 20 30 40 50 60 MSQLFNFSAG PAMLPVDVLK QAQEELLNWN GQGVSVMEIS HRDPVYVHMA REAEQDLRDL 70 80 90 100 110 120 LNVPDDYEVL FLQGGGRGQF SAVPQNIASP DATVDYLDTG IWSGFAIREA EKFVSKVNVA 130 140 150 160 170 180 GQVQEGAKGK EIQSPENWKL SENAAYFHYC PNETVDGIAL HEIPDVKAPI VADMSSNILS 190 200 210 220 230 240 EPLDVSKFGV IYAGAQKNIG PSGFAIAIVK KSLLGHPQKQ VSSIMDYQLQ AKDGSMYNTP 250 260 270 280 290 300 NTFAWYLAGL VFKWLKAQGG LTAMGERNRH KAQLLYDFVD KSDFYRNDIN PAYRSIMNIP 310 320 330 340 350 360 FQLAYDKLDA EFLQGAKNQG LLGLKGHRFV GGMRASIYNA MPVEGVEALL NYMADFERKL G

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017340 Genomic DNA. Translation: AAV82199.1.
RefSeq	YP_155748.1. NC_006512.1.
3D structure databases
ProteinModelPortal	Q5QZ48.
SMR	Q5QZ48. Positions 3-361.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3173560.
GenomeReviews	Gene locus IL1359 in contig AE017340_GR.
KEGG	ilo:IL1359.
NMPDR	fig|283942.3.peg.1611.
PATRIC	22140793. VBIIdiLoi21852_1360.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289982.
OMA	YEVLFLQ.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	ILOI283942:IL1359-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_IDILO

Accession

Primary (citable) accession number: Q5QZ48

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program