Q59196 (SERC_BACCI) 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

Organism

Bacillus circulans

Taxonomic identifier

1397 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. Ref.5
Catalytic activity	O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. Ref.2 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. Ref.2
Cofactor	Binds 1 pyridoxal phosphate per subunit. Ref.4 Ref.5
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. Ref.2 Ref.5
Subcellular location	Cytoplasm By similarity HAMAP MF_00160.
Miscellaneous	Significant conformational rearrangements are involved in response to pH changes. HAMAP MF_00160
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Biophysicochemical properties	Kinetic parameters: KM=1 mM for glutamate (at pH 7) Ref.5 KM=0.2 mM for glutamate (at pH 9) KM=0.1 mM for phosphohydroxypyruvate (at pH 7) KM=0.09 mM for phosphohydroxypyruvate (at pH 9) Vmax=6 nmol/min/mg enzyme for the reaction forming phosphoserine (at pH 7) Vmax=10 nmol/min/mg enzyme for the reaction forming phosphoserine (at pH 9) pH dependence: Optimum pH is 9.0. At pH 9.5, retains more 60% of its maximum activity. Inactive below pH 6. Temperature dependence: Thermal denaturation midpoint (Tm) is 71 degrees Celsius at pH 6 and is lowered around 58 degrees Celsius at pH 8.5 and 10.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	L-serine 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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 362

361

Phosphoserine aminotransferase HAMAP MF_00160

PRO_0000150147

Regions

Region

77 – 78

2

Pyridoxal phosphate binding HAMAP MF_00160

Region

238 – 239

2

Pyridoxal phosphate binding HAMAP MF_00160

Sites

Binding site

43

1

L-glutamate By similarity

Binding site

103

1

Pyridoxal phosphate

Binding site

153

1

Pyridoxal phosphate

Binding site

173

1

Pyridoxal phosphate

Binding site

196

1

Pyridoxal phosphate

Amino acid modifications

Modified residue

197

1

N6-(pyridoxal phosphate)lysine HAMAP MF_00160

Secondary structure

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362

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Helix

17 – 25

9

Beta strand

27 – 30

4

Beta strand

33 – 35

3

Helix

37 – 39

3

Helix

45 – 61

17

Beta strand

66 – 75

10

Helix

76 – 88

13

Beta strand

94 – 99

6

Helix

102 – 114

13

Beta strand

117 – 122

6

Helix

124 – 126

3

Helix

134 – 136

3

Beta strand

143 – 152

10

Turn

153 – 156

4

Beta strand

170 – 173

4

Turn

175 – 179

5

Helix

185 – 187

3

Beta strand

189 – 194

6

Turn

195 – 199

5

Beta strand

205 – 210

6

Helix

211 – 213

3

Beta strand

214 – 216

3

Helix

223 – 225

3

Helix

227 – 232

6

Turn

233 – 235

3

Helix

242 – 257

16

Helix

260 – 280

21

Beta strand

285 – 290

6

Helix

292 – 294

3

Beta strand

297 – 303

7

Helix

307 – 319

13

Beta strand

322 – 324

3

Turn

329 – 331

3

Beta strand

333 – 337

5

Helix

344 – 361

18

Sequences

	Sequence		Length	Mass (Da)
	Q59196 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2D63C629C8DD269B	FASTA	362	39,924
	10 20 30 40 50 60 MSKRAYNFNA GPAALPLEVL ERAQAEFVDY QHTGMSIMEM SHRGAVYEAV HNEAQARLLA 70 80 90 100 110 120 LLGNPTGYKV LFIQGGASTQ FAMIPMNFLK EGQTANYVMT GSWASKALKE AKLIGDTHVA 130 140 150 160 170 180 ASSEASNYMT LPKLQEIQLQ DNAAYLHLTS NETIEGAQFK AFPDTGSVPL IGDMSSDILS 190 200 210 220 230 240 RPFDLNQFGL VYAGAQKNLG PSGVTVVIVR EDLVAESPKH LPTMLRYDTY VKNNSLYNTP 250 260 270 280 290 300 PSFGIYMVNE VLKWIEERGG LEGVQQANRK KASLIYDAID QSGGFYRGCV DVDSRSDMNI 310 320 330 340 350 360 TFRLASEELE KEFVKASEQE GFVGLKGHRS VGGLRASIYN AVPYESCEAL VQFMEHFKRS RG

References

[1]	"Phosphoserine aminotransferase from Bacillus circulans var. alkalophilus: purification, gene cloning and sequencing." Battchikova N., Holopainen M., Himanen J.-P., Korpela T. (In) Sannia G. (eds.); Proceedings of 9th meeting on vitamin B6 and carbonyl catalysis, pp.207-207, Dipt. Chimica Organica e Biologica, Napoli (1994) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 21783 / subsp. Alkalophilus.
[2]	"Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing." Battchikova N., Himanen J.-P., Ahjolahti M., Korpela T. Biochim. Biophys. Acta 1295:187-194(1996) [PubMed: 8695645] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, SUBUNIT, CATALYTIC ACTIVITY. Strain: ATCC 21783 / subsp. Alkalophilus.
[3]	"Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus." Moser M., Mueller R., Battchikova N., Koivulehto M., Korpela T., Jansonius J.N. Protein Sci. 5:1426-1428(1996) [PubMed: 8819175] [Abstract] Cited for: CRYSTALLIZATION. Strain: ATCC 21783 / subsp. Alkalophilus.
[4]	Hester G., Luong T.N., Moser M., Jansonius J.N. Submitted (SEP-1998) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLU-3 IN COMPLEX WITH PLP, COFACTOR. Strain: ATCC 21783 / subsp. Alkalophilus.
[5]	"Effect of pH on the structure and stability of Bacillus circulans ssp. alkalophilus phosphoserine aminotransferase: thermodynamic and crystallographic studies." Kapetaniou E.G., Thanassoulas A., Dubnovitsky A.P., Nounesis G., Papageorgiou A.C. Proteins 63:742-753(2006) [PubMed: 16532449] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF MUTANT GLU-3 IN COMPLEX WITH PLP, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. Strain: ATCC 21783 / subsp. Alkalophilus.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z46432 Genomic DNA. Translation: CAA86558.2.

PIR

S71439.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BT4	X-ray	2.30	A	1-362	[»]
1W3U	X-ray	1.50	A	1-362	[»]
2C0R	X-ray	1.20	A/B	1-362	[»]

ProteinModelPortal

Q59196.

SMR

Q59196. Positions 2-362.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

2.6.1.52. 649.

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.

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_BACCI

Accession

Primary (citable) accession number: Q59196

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	October 19, 2011
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program