NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1007/s00203-004-0742-9; PubMed=15551059 [NCBI, ExPASy, EBI, Israel, Japan]
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.;
"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1.";
Arch. Microbiol. 183:27-36(2005).

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.
CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
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 .
PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CR555306; CAI06614.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_157515.1; -.

3D structure databases

ModBase

Q5P7U7.

Enzyme and pathway databases

BioCyc

ASP76114:EBA907-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004648;	Molecular function: phosphoserine transaminase activity (inferred from electronic annotation from HAMAP).
GO:0030170;	Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from HAMAP).
GO:0006564;	Biological process: L-serine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008615;	Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00160; -; 1.
PBIL [Tree]

InterPro

IPR000192; Aminotrans_V/Cys_dSase.
IPR003248; Pser_amintransf.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
IPR015422; PyrdxlP-dep_Trfase_major_sub2.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.

Pfam

PF00266; Aminotran_5; 1.
Pfam graphical view of domain structure.

ProDom

PD001544; Pser_amintransf; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01364; serC_1; 1.

PROSITE

PS00595; AA_TRANSFER_CLASS_5; FALSE_NEG.

ProtoNet

Q5P7U7.

Genome annotation databases

GeneID

3182379; -.

GenomeReviews

CR555306_GR; AZOSEA04920.

KEGG

eba:ebA907; -.

NMPDR

fig|76114.4.peg.1425; -.

Phylogenomic databases

HOGENOM

Q5P7U7; -.

Genome annotation databases

CMR

Q5P7U7; AZOSEA04920.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis; Serine biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 366`	`366`	`Phosphoserine aminotransferase.`	`PRO_0000150143`
`REGION`	`76 77`	`2`	`Pyridoxal phosphate binding (By similarity).`
`REGION`	`243 244`	`2`	`Pyridoxal phosphate binding (By similarity).`
`BINDING`	`42 42`		`L-glutamate (By similarity).`
`BINDING`	`101 101`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`156 156`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`178 178`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`201 201`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`202 202`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 366 AA [This is the length of the unprocessed precursor]

Molecular weight: 39471 Da [This is the MW of the unprocessed precursor]

CRC64: 98F0A61E37A1EF0F [This is a checksum on the sequence]

        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

Q5P7U7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools