Reviewed, UniProtKB/Swiss-Prot Q5P7U7 (SERC_AZOSE)

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:	AZOSEA04920
ORF Names:	ebA907

Organism

Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]

Taxonomic identifier

76114 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length	366 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 – 366	366	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150143
Regions
	Region	76 – 77	2	Pyridoxal phosphate binding By similarity
	Region	243 – 244	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	42	1	L-glutamate By similarity
	Binding site	101	1	Pyridoxal phosphate By similarity
	Binding site	156	1	Pyridoxal phosphate By similarity
	Binding site	178	1	Pyridoxal phosphate By similarity
	Binding site	201	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	202	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P7U7-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 98F0A61E37A1EF0F	FASTA	366	39,471
	10 20 30 40 50 60 MTRVYNFSAG PAALPEAVLQ QAAEEMLDWQ GAGCGVMEMS HRGKEFTSIV AQAEADLREL 70 80 90 100 110 120 LAIPDNYRVL FLQGGATQQF AQIPMNLLAG GSADYLVTGS WSKKAYGEAK HLAGALGGAV 130 140 150 160 170 180 RLAGSTETAG FTRLLRTEEL DLDPRARYLH LCTNETIHGV ELCEVSRLPD TGVPLVADMS 190 200 210 220 230 240 SHILSRPLDI GRYGLIYAGA QKNIGPSGLV VVIVREDLLG HASPVTPTIM DYRVMAENGS 250 260 270 280 290 300 MLNTPPTYAI YIAGLVFRWL KAQGGLAAVE ANNIAKSDLL YDFLDASDFY ENRVAQDSRS 310 320 330 340 350 360 RMNIPFLLRD DALNDPFLAG AKAAGLTQLK GHKSVGGMRA SIYNAMPLAG VQALVDYMRD FSARNG

References

[1]	"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1." Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R. Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR555306 Genomic DNA. Translation: CAI06614.1.
RefSeq	YP_157515.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P7U7.
Genome annotation databases
GeneID	3182379.
GenomeReviews	Gene locus AZOSEA04920 in contig CR555306_GR.
KEGG	eba:ebA907.
NMPDR	fig|76114.4.peg.1425.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5P7U7.
OMA	SMYNTPP.
Enzyme and pathway databases
BioCyc	ASP76114:EBA907-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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_AZOSE

Accession

Primary (citable) accession number: Q5P7U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 40 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)