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.

ProtoNet

P44336.

Genome annotation databases

949636; -.

L42023_GR; HI1167.

hin:HI1167; -.

fig|71421.1.peg.1120; -.

TIGR

HI1167; -.

Phylogenomic databases

HOGENOM

P44336; -.

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`	`1 362`	`362`	`Phosphoserine aminotransferase.`	`PRO_0000150174`
`REGION`	`76 77`	`2`	`Pyridoxal phosphate binding (By similarity).`
`REGION`	`237 238`	`2`	`Pyridoxal phosphate binding (By similarity).`
`BINDING`	`42 42`		`L-glutamate (By similarity).`
`BINDING`	`102 102`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`152 152`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`172 172`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`195 195`		`Pyridoxal phosphate (By similarity).`
`BINDING`	`196 196`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 362 AA [This is the length of the unprocessed precursor]

Molecular weight: 40313 Da [This is the MW of the unprocessed precursor]

CRC64: 1DBDC9F25B76C3F7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQVFNFSAG PAMIFPEVLQ KAQNELINWL NQGVSVMEVS HRGKYFMELV TQAEKDLREV 

        70         80         90        100        110        120 
YNIPDNYRTL FLQGGARGQF ATIPMNLIGK KGKALYLNSG HWSATAAKEA RNFAEIDEIT 

       130        140        150        160        170        180 
IVENGEQTRI TDLDFSHIAD QYDYVHYCPN ETISGVEIFD VPNVGNAVLV ADMSSNILSR 

       190        200        210        220        230        240 
QIDISKFGVI YAGAQKNLGP AGITLVIIRD DLIGNARKET PSIWNYATQR DADSMINTPP 

       250        260        270        280        290        300 
TFAWYLCSLV FKHLKEIGGL EIIEKRNALK AQTLYDYIDS SKLYRNVVAK ENRSTMNVTF 

       310        320        330        340        350        360 
ITGNPELDAK FVAESTAAGL QALKGHKVLG GMRASIYNAM SQNGVEALIS FMKKFETENL 


PQ

P44336 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