Q2SCF2 (SERC_HAHCH) 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
Ordered Locus Names:	HCH_04982

Organism

Hahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]

Taxonomic identifier

349521 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Hahellaceae › Hahella › Hahella chejuensis

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity. HAMAP-Rule MF_00160
Catalytic activity	O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP-Rule MF_00160 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP-Rule MF_00160
Cofactor	Binds 1 pyridoxal phosphate per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP-Rule MF_00160 Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP-Rule MF_00160
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Pyridoxine biosynthesis Serine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	L-serine biosynthetic process Inferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic process Inferred from electronic annotation. Source: HAMAP
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: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: HAMAP
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-Rule MF_00160		PRO_1000123469
Regions
	Region	238 – 239	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	43	1	L-glutamate By similarity
	Binding site	103	1	Pyridoxal phosphate By similarity
	Binding site	153	1	Pyridoxal phosphate By similarity
	Binding site	173	1	Pyridoxal phosphate By similarity
	Binding site	196	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	197	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2SCF2 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 63AAE8DC2F5DDDA4	FASTA	361	39,513
	10 20 30 40 50 60 MADRKFNFCA GPSALPTEVL LQAQAELLDW RGKGLSIMEM SHRSDDFVAV AVEAERDFRE 70 80 90 100 110 120 LMSVPDNYKV LFVQGGAATQ FASVPLNLLK LGAEADYIDT GIWSKKAIAE AGRYLKVNVA 130 140 150 160 170 180 ASAKDNGYAC IPARSEWRLS ESAGYVHYTP NETIGGVEFL DIPDVGDKPL VADMSSTILS 190 200 210 220 230 240 RPVDISRFGV IYAGAQKNIG PAGLTLVIVR EDLLGYASDS LPTMLNYKVA SENDSMVNTP 250 260 270 280 290 300 PTFSWYLAGL VFKWLKGKGG VQAMEAINCR KADKLYSYID DSEFYANPID LSCRSWMNVP 310 320 330 340 350 360 FTLKDDRLDQ KFLQEAEGAG LLNLQGHRSV GGMRASLYNA LPEEAVDALI GFMQDFAGRN A

References

[1]

"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent." Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F. Nucleic Acids Res. 33:7066-7073(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KCTC 2396.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000155 Genomic DNA. Translation: ABC31672.1.
RefSeq	YP_436097.1. NC_007645.1.
3D structure databases
HSSP	HSSP built from PDB template 2C0R based on UniProtKB Q59196.
ProteinModelPortal	Q2SCF2.
SMR	Q2SCF2. Positions 4-361.
ModBase	Search...
Protein-protein interaction databases
STRING	349521.HCH_04982.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3843079.
KEGG	hch:HCH_04982.
PATRIC	22090356. VBIHahChe29232_4532.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1932.
HOGENOM	HOG000088965.
KO	K00831.
OMA	MSIMEMS.
ProtClustDB	PRK05355.
Enzyme and pathway databases
BioCyc	HCHE349521:GHAL-4831-MONOMER.
UniPathway	UPA00135; UER00197. UPA00244; UER00311.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
HAMAP	MF_00160. SerC_aminotrans_5.
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR022278. Pser_aminoTfrase. IPR003248. Pser_aminoTfrase_subgr. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
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_HAHCH

Accession

Primary (citable) accession number: Q2SCF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program