Q6A9B0 (MEND_PROAC) 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:	PPA0903

Organism

Propionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]

Taxonomic identifier

267747 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium › Propionibacterium acnes

Protein attributes

Sequence length	508 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.
Sequence caution	The sequence AAT82656.1 differs from that shown. Reason: Erroneous initiation.

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 – 508	508	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659		PRO_0000341809

Sequences

	Sequence		Length	Mass (Da)
	Q6A9B0 [UniParc]. Last modified July 1, 2008. Version 2. Checksum: B9ADC09A593370E0	FASTA	508	53,075
	10 20 30 40 50 60 MNPSTAVARR LVNALVEAGV EHVVYCPGSR DAPIGYALAD AETAGWLRVY VRLDERSAGF 70 80 90 100 110 120 VALGLGRAGC PAALVTTSGT AVANIHPAVL EADAAGVPLI VLSADRPAEM WHTGANQTTV 130 140 150 160 170 180 QTGIFGSAPR LSTDVPAGFP ADERLDALVL RAVTAATGAL SADPGPVHLN VSFRDSLVPD 190 200 210 220 230 240 GPWQPQALVP RRVSSFPTAP TPLVMPARTV VVAGDGAGSL ARELAQQGGW PLLAEPTSGS 250 260 270 280 290 300 RVGDNALTDY QTVLGSELVD DVEAVLVLGH PTLSRPVSRL LARPDVTVVT DRSRWTDVAG 310 320 330 340 350 360 VARVVTGPVE LAEIDTDPAW LGRWKDADRP VVPTAKQRLC RDIWWACTTP NAPVLVIGAS 370 380 390 400 410 420 EVIRCFDRFA VPGDIAPTAL ANRGLAGIDG TIATAIGVGL GTGRPVRVVV GDLTFAHDAM 430 440 450 460 470 480 SLLLGETEPE PDVQVVVLDD RGGAIFSGLE HAAAPAPVLR RMFLTPQRLD SAALAHALGA 490 500 SHRRVSPDDL QFLDEPVVGR QVVSVPLT

References

[1]

"The complete genome sequence of Propionibacterium acnes, a commensal of human skin." Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G. Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017283 Genomic DNA. Translation: AAT82656.1. Different initiation.
RefSeq	YP_055614.1. NC_006085.1.
3D structure databases
ProteinModelPortal	Q6A9B0.
ModBase	Search...
Protein-protein interaction databases
STRING	267747.PPA0903.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT82656; AAT82656; PPA0903.
GeneID	2930918.
KEGG	pac:PPA0903.
PATRIC	23036523. VBIProAcn64440_0936.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1165.
HOGENOM	HOG000218359.
KO	K02551.
OMA	ANRPYEM.
ProtClustDB	CLSK2763589.
Enzyme and pathway databases
BioCyc	PACN267747:GHO9-952-MONOMER.
UniPathway	UPA00079; UER00164.
Family and domain databases
HAMAP	MF_01659. MenD.
InterPro	IPR004433. MenaQ_synth_MenD. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. IPR011766. TPP_enzyme-bd_C. [Graphical view]
PANTHER	PTHR18968:SF3. PTHR18968:SF3. 1 hit.
Pfam	PF02775. TPP_enzyme_C. 1 hit. 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_PROAC

Accession

Primary (citable) accession number: Q6A9B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	July 1, 2008
Last modified:	May 1, 2013
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program