A1KG32 (MEND_MYCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
Short name=SEPHCHC synthase
EC=2.2.1.9

Alternative name(s):
Menaquinone biosynthesis protein MenD

Gene names

Name:	menD
Ordered Locus Names:	BCG_0600

Organism

Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]

Taxonomic identifier

410289 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis › Mycobacterium bovis BCG

Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) By similarity. HAMAP-Rule MF_01659
Catalytic activity	Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2. HAMAP-Rule MF_01659
Cofactor	Magnesium or manganese By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Pathway	Cofactor biosynthesis; menaquinone biosynthesis; menaquinone-2 from chorismate: step 2/8. HAMAP-Rule MF_01659
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the TPP enzyme family. MenD subfamily.

Ontologies

Keywords
Biological process	Menaquinone biosynthesis
Ligand	Magnesium Manganese Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	menaquinone biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP thiamine pyrophosphate 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 – 554	554	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659		PRO_0000341776

Sequences

	Sequence		Length	Mass (Da)
	A1KG32 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 879423AAB00F36A5	FASTA	554	57,836
	10 20 30 40 50 60 MNPSTTQARV VVDELIRGGV RDVVLCPGSR NAPLAFALQD ADRSGRIRLH VRIDERTAGY 70 80 90 100 110 120 LAIGLAIGAG APVCVAMTSG TAVANLGPAV VEANYARVPL IVLSANRPYE LLGTGANQTM 130 140 150 160 170 180 EQLGYFGTQV RASISLGLAE DAPERTSALN ATWRSATCRV LAAATGARTA NAGPVHFDIP 190 200 210 220 230 240 LREPLVPDPE PLGAVTPPGR PAGKPWTYTP PVTFDQPLDI DLSVDTVVIS GHGAGVHPNL 250 260 270 280 290 300 AALPTVAEPT APRSGDNPLH PLALPLLRPQ QVIMLGRPTL HRPVSVLLAD AEVPVFALTT 310 320 330 340 350 360 GPRWPDVSGN SQATGTRAVT TGAPRPAWLD RCAAMNRHAI AAVREQLAAH PLTTGLHVAA 370 380 390 400 410 420 AVSHALRPGD QLVLGASNPV RDVALAGLDT RGIRVRSNRG VAGIDGTVST AIGAALAYEG 430 440 450 460 470 480 AHERTGSPDS PPRTIALIGD LTFVHDSSGL LIGPTEPIPR SLTIVVSNDN GGGIFELLEQ 490 500 510 520 530 540 GDPRFSDVSS RIFGTPHDVD VGALCRAYHV ESRQIEVDEL GPTLDQPGAG MRVLEVKADR 550 SSLRQLHAAI KAAL

References

[1]

"Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM408590 Genomic DNA. Translation: CAL70585.1.
RefSeq	YP_976696.1. NC_008769.1.
3D structure databases
ProteinModelPortal	A1KG32.
SMR	A1KG32. Positions 1-547.
ModBase	Search...
Protein-protein interaction databases
STRING	410289.BCG_0600.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL70585; CAL70585; BCG_0600.
GeneID	4697151.
KEGG	mbb:BCG_0600.
PATRIC	18011735. VBIMycBov80988_0647.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1165.
HOGENOM	HOG000218359.
KO	K02551.
OMA	ANRPYEM.
ProtClustDB	PRK07449.
Enzyme and pathway databases
BioCyc	MBOV410289:GJW7-606-MONOMER.
UniPathway	UPA00079; UER00164.
Family and domain databases
HAMAP	MF_01659. MenD.
InterPro	IPR004433. MenaQ_synth_MenD. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. [Graphical view]
PANTHER	PTHR18968:SF3. PTHR18968:SF3. 1 hit.
Pfam	PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
PIRSF	PIRSF004983. MenD. 1 hit.
TIGRFAMs	TIGR00173. menD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MEND_MYCBP

Accession

Primary (citable) accession number: A1KG32

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program