Reviewed, UniProtKB/Swiss-Prot P63515 (SERC_MYCBO)

Names and origin

Protein names

Recommended name:
    Putative phosphoserine aminotransferase
    EC=2.6.1.52
Alternative name(s):
    Phosphohydroxythreonine aminotransferase
      Short name=PSAT

Gene names

Name:	serC
Ordered Locus Names:	Mb0908c

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glyceric acid: 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 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: 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: 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 – 376	376	Putative phosphoserine aminotransferase HAMAP MF_00160		PRO_0000150189
Regions
	Region	84 – 85	2	Pyridoxal phosphate binding By similarity
	Region	251 – 252	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	50	1	L-glutamate By similarity
	Binding site	108	1	Pyridoxal phosphate By similarity
	Binding site	154	1	Pyridoxal phosphate By similarity
	Binding site	176	1	Pyridoxal phosphate By similarity
	Binding site	199	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	200	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63515-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 32677398E8967D1E	FASTA	376	40,233
	10 20 30 40 50 60 MADQLTPHLE IPTAIKPRDG RFGSGPSKVR LEQLQTLTTT AAALFGTSHR QAPVKNLVGR 70 80 90 100 110 120 VRSGLAELFS LPDGYEVILG NGGATAFWDA AAFGLIDKRS LHLTYGEFSA KFASAVSKNP 130 140 150 160 170 180 FVGEPIIITS DPGSAPEPQT DPSVDVIAWA HNETSTGVAV AVRRPEGSDD ALVVIDATSG 190 200 210 220 230 240 AGGLPVDIAE TDAYYFAPQK NFASDGGLWL AIMSPAALSR IEAIAATGRW VPDFLSLPIA 250 260 270 280 290 300 VENSLKNQTY NTPAIATLAL LAEQIDWLVG NGGLDWAVKR TADSSQRLYS WAQERPYTTP 310 320 330 340 350 360 FVTDPGLRSQ VVGTIDFVDD VDAGTVAKIL RANGIVDTEP YRKLGRNQLR VAMFPAVEPD 370 DVSALTECVD WVVERL

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX248336 Genomic DNA. Translation: CAD93769.1.
RefSeq	NP_854565.1.
3D structure databases
SMR	P63515. Positions 8-376.
ModBase	Search...
Genome annotation databases
GeneID	1092794.
GenomeReviews	Gene locus Mb0908c in contig BX248333_GR.
KEGG	mbo:Mb0908c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P63515.
OMA	P63515. RDAPPGL.
Enzyme and pathway databases
BRENDA	2.6.1.52. 3091.
Family and domain databases
HAMAP	MF_00160. [Tree]
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR006272. Ser_trans_bac. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01366. serC_3. 1 hit.
PROSITE	PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SERC_MYCBO

Accession

Primary (citable) accession number: P63515
Secondary accession number(s): Q10534

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 38 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)