Reviewed, UniProtKB/Swiss-Prot Q6HGI0 (SERC_BACHK)

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:	BT9727_3023

Organism

Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]

Taxonomic identifier

180856 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	360 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 MF_00160
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 By similarity. HAMAP MF_00160
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160
Subunit structure	Homodimer By similarity. HAMAP MF_00160
Subcellular location	Cytoplasm By similarity HAMAP MF_00160.
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Ontologies

Keywords
Biological process	Amino-acid 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
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 – 360	360	Phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150151
Regions
	Region	76 – 77	2	Pyridoxal phosphate binding By similarity
	Region	237 – 238	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	42	1	L-glutamate By similarity
	Binding site	102	1	Pyridoxal phosphate By similarity
	Binding site	152	1	Pyridoxal phosphate By similarity
	Binding site	172	1	Pyridoxal phosphate By similarity
	Binding site	195	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	196	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HGI0-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 7463052C1486E016	FASTA	360	40,366
	10 20 30 40 50 60 MERVYNFSAG PSILPLPVLE KVQKELVNYN GTGMSIMEMS HRSSYFQSII DEAGSLLREL 70 80 90 100 110 120 MNIPDEYEVL FLQGGASLQF SMIPLNLMNT YKKAGYVLTG SWSKKALQEA EKVGEVQVIA 130 140 150 160 170 180 SSENEKFTTI PKLDGLLGNE KLDYVHITTN NTIEGTKYVD IPHVDKVPLV ADMSSNILSE 190 200 210 220 230 240 RYDVSKFGLI YAGAQKNLGP AGLTIAIIKR DLIGGADRYC PTMLNYETYS KNNSLYNTPP 250 260 270 280 290 300 SFSIYVTKIV LEWLKEQGGV SAIEEQNKMK SSLLYNFLDE SKLFTSPVDP TYRSLMNIPF 310 320 330 340 350 360 TTPSEELNNE FLQKAKERGL VTLKGHRSVG GMRASIYNAM PAHGVQQLVN YMKEFELENR

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT62315.1.
RefSeq	YP_037346.1.
3D structure databases
SMR	Q6HGI0. Positions 1-356.
ModBase	Search...
Genome annotation databases
GeneID	2855750.
GenomeReviews	Gene locus BT9727_3023 in contig AE017355_GR.
KEGG	btk:BT9727_3023.
NMPDR	fig|281309.1.peg.2986.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289982.
OMA	TFAWYLA.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_3023-MONOMER.
Family and domain databases
HAMAP	MF_00160. SerC_aminotrans_5. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR003248. Pser_amintransf. 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.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01364. serC_1. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_BACHK

Accession

Primary (citable) accession number: Q6HGI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)