Q9RME2 (SERC_BACAO) 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 alcalophilus

Taxonomic identifier

1445 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
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.2
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. Ref.3 Ref.4
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160
Subunit structure	Homodimer. Ref.2 Ref.3
Subcellular location	Cytoplasm By similarity HAMAP MF_00160.
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 9.0. At pH 9.5, retains more than 60% of its maximum activity. At pH 7.0 the relative activity is less than 10%. HAMAP MF_00160

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure
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

Chain

1 – 361

361

Phosphoserine aminotransferase HAMAP MF_00160

PRO_0000293583

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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361

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 – 62

18

Beta strand

68 – 75

8

Helix

76 – 88

13

Beta strand

94 – 99

6

Helix

102 – 112

11

Beta strand

115 – 122

8

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 – 214

4

Helix

223 – 225

3

Helix

227 – 232

6

Turn

233 – 235

3

Helix

242 – 257

16

Helix

260 – 280

21

Turn

281 – 284

4

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 – 360

17

Sequences

	Sequence		Length	Mass (Da)
	Q9RME2 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C4D48D1785C60A85	FASTA	361	40,335
	10 20 30 40 50 60 MVKQVFNFNA GPSALPKPAL ERAQKELLNF NDTQMSVMEL SHRSQSYEEV HEQAQNLLRE 70 80 90 100 110 120 LLQIPNDYQI LFLQGGASLQ FTMLPMNLLT KGTIGNYVLT GSWSEKALKE AKLLGETHIA 130 140 150 160 170 180 ASTKANSYQS IPDFSEFQLN ENDAYLHITS NNTIYGTQYQ NFPEINHAPL IADMSSDILS 190 200 210 220 230 240 RPLKVNQFGM IYAGAQKNLG PSGVTVVIVK KDLLNTKVEQ VPTMLQYATH IKSDSLYNTP 250 260 270 280 290 300 PTFSIYMLRN VLDWIKDLGG AEAIAKQNEE KAKIIYDTID ESNGFYVGHA EKGSRSLMNV 310 320 330 340 350 360 TFNLRNEELN QQFLAKAKEQ GFVGLNGHRS VGGCRASIYN AVPIDACIAL RELMIQFKEN A

References

[1]	"Phosphoserine aminotransferase from obligate alkalophile Bacillus alcalophilus." Battchikova N.V., Koivulehto M.K. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27647 / DSM 485 / JCM 5262 / NCTC 4553.
[2]	"Expression, purification, crystallization and preliminary crystallographic analysis of phosphoserine aminotransferase from Bacillus alcalophilus." Dubnovitsky A.P., Kapetaniou E.G., Papageorgiou A.C. Acta Crystallogr. D 59:2319-2321(2003) [PubMed: 14646107] [Abstract] Cited for: FUNCTION, SUBUNIT, CRYSTALLIZATION. Strain: ATCC 27647 / DSM 485 / JCM 5262 / NCTC 4553.
[3]	"Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus." Dubnovitsky A.P., Kapetaniou E.G., Papageorgiou A.C. Protein Sci. 14:97-110(2005) [PubMed: 15608117] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) IN COMPLEX WITH PLP, SUBUNIT, COFACTOR, PH DEPENDENCE. Strain: ATCC 27647 / DSM 485 / JCM 5262 / NCTC 4553.
[4]	"Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage." Dubnovitsky A.P., Ravelli R.B.G., Popov A.N., Papageorgiou A.C. Protein Sci. 14:1498-1507(2005) [PubMed: 15883191] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH PLP, COFACTOR. Strain: ATCC 27647 / DSM 485 / JCM 5262 / NCTC 4553.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF204962 Genomic DNA. Translation: AAF13453.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W23	X-ray	1.08	A/B	2-361	[»]
2BHX	X-ray	1.68	A/B	2-361	[»]
2BI1	X-ray	1.69	A/B	2-361	[»]
2BI2	X-ray	1.69	A/B	2-361	[»]
2BI3	X-ray	1.69	A/B	2-361	[»]
2BI5	X-ray	1.73	A/B	2-361	[»]
2BI9	X-ray	1.73	A/B	2-361	[»]
2BIA	X-ray	1.77	A/B	2-361	[»]
2BIE	X-ray	1.30	A/B	1-361	[»]
2BIG	X-ray	1.30	A/B	1-361	[»]

ProteinModelPortal

Q9RME2.

SMR

Q9RME2. Positions 2-361.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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_BACAO

Accession

Primary (citable) accession number: Q9RME2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	May 1, 2000
Last modified:	October 19, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program