B0RCZ5 (MEND_CLAMS) 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:	CMS3017

Organism

Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / JCM 9667) [Complete proteome] [HAMAP]

Taxonomic identifier

31964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Clavibacter › Clavibacter michiganensis

Protein attributes

Sequence length	589 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. HAMAP-Rule MF_01659 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. HAMAP-Rule MF_01659
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 – 589	589	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659		PRO_0000341725

Sequences

	Sequence		Length	Mass (Da)
	B0RCZ5 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: 82920B3D1DDA1B78	FASTA	589	61,555
	10 20 30 40 50 60 MAAADALPTS SASASASADG PRTGNPSTDR AIAMLLALVR EGVTDVVLCP GSRSQALALV 70 80 90 100 110 120 AAELERVDGV RLHVRIDERA AGFLALGLGV ESGRPAPVIT TSGTAVANLH PAVLEGWHSG 130 140 150 160 170 180 VPMLLLTGDR PAELRGIASN QTTRQPGMFG DRVACIDVPA PEETDDDLAR DALLARDAYR 190 200 210 220 230 240 RARDERTPVH VNVAFRDPLS VAVPDLTEAV AEVRAAAPAT PAPAGPATAD VLDLPHGPRT 250 260 270 280 290 300 LVVAGHAAGE AAEELARAGG WPLAAEISSG SHFGPNLVVS FRELLAREGF GDRVERVIVF 310 320 330 340 350 360 GHPTLTREVP LLVGREDVEA IVVGSTGGED YDPRHRVTAH PAAVRVVGEP ADPAEARRWL 370 380 390 400 410 420 GTWVHESRAI LDEATAAESA PLLPSGTTPA ERRDFARAEL AAVRADVTRR HLVRALWQAT 430 440 450 460 470 480 WPHDRLVLGA SRLIREADRA LPGKRVRVHA NRGLAGIDGT ISTGLGIALA SQAGSGSAAA 490 500 510 520 530 540 GITRVLVGDL TLLHDVGSLL IGTGERVPRI QVIVGNDGGG TIFDGLEVSR TAAPASIDRV 550 560 570 580 MFTPQRVDLA SLARAYGWAH LRAATHGELE AALTTASEAP LLIEVPLAR

References

[1]

"Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. sepedonicus suggests recent niche adaptation." Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., Parkhill J., Ishimaru C.A. J. Bacteriol. 190:2150-2160(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33113 / JCM 9667.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM849034 Genomic DNA. Translation: CAQ03087.1.
RefSeq	YP_001711643.1. NC_010407.1.
3D structure databases
ProteinModelPortal	B0RCZ5.
ModBase	Search...
Protein-protein interaction databases
STRING	31964.CMS_3017.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAQ03087; CAQ03087; CMS3017.
GeneID	6158519.
KEGG	cms:CMS_3017.
PATRIC	21463057. VBIClaMic4666_3062.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1165.
KO	K02551.
OMA	ANRPYEM.
ProtClustDB	CLSK821548.
Enzyme and pathway databases
BioCyc	CMIC31964:GJBN-3011-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_CLAMS

Accession

Primary (citable) accession number: B0RCZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	April 8, 2008
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program