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; 1.

Genome annotation databases

GeneID

2879293; -.

GenomeReviews

CR543861_GR; ACIAD2647.

KEGG

aci:ACIAD2647; -.

NMPDR

fig|62977.3.peg.2419; -.

Phylogenomic databases

HOGENOM

Q6F961; -.

Genome annotation databases

CMR

Q6F961; ACIAD2647.

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`	`1 359`	`359`	`Phosphoserine aminotransferase.`	`PRO_0000150142`
`REGION`	`75 76`	`2`	`Pyridoxal phosphate binding (By similarity).`
`REGION`	`236 237`	`2`	`Pyridoxal phosphate binding (By similarity).`
`BINDING`	`41 41`		`L-glutamate (By similarity).`
`BINDING`	`101 101`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`152 152`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`171 171`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`194 194`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`195 195`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 359 AA [This is the length of the unprocessed precursor]

Molecular weight: 39329 Da [This is the MW of the unprocessed precursor]

CRC64: 91B7C48816B85F89 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRAYNFCAGP AALPTAVLEK AQQELLDWQG KGLSIMEMSH RSKDYVAVAE KAEADLRKLM 

        70         80         90        100        110        120 
NIPENYQVLF LQGGASLQFS AIPMNLLGKN SKADYIHTGI WSEKALKEAQ RYGDINVIEA 

       130        140        150        160        170        180 
GTSIDGKLAI KNQSEWNLSQ DAAYVHYAEN ETIGGIQFAD IPDVNVPLVS DLSSSILSAP 

       190        200        210        220        230        240 
LDVSKFGLIY AGAQKNIGPA GLTIVIVRDD LLDQSRSDIP SILKYSAQAK NGSMVNTPAT 

       250        260        270        280        290        300 
YAWYLSGLVF EWLLEQGGVD AIHQVNLEKA KLLYGYIDSS DFYNNPIAVP NRSIMNVPFT 

       310        320        330        340        350 
LADEALEKLF LQEAEENHLL NLAGHRSVGG MRASIYNAVP LEGVQALVNF MDTFVQKHG

Q6F961 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