Q0I316 (MEND_HAES1) 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:	HS_0617

Organism

Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]

Taxonomic identifier

205914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Histophilus › Haemophilus somnus

Protein attributes

Sequence length	568 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 – 568	568	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659		PRO_0000341756

Sequences

	Sequence		Length	Mass (Da)
	Q0I316 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 83A7C0CCC0908D3A	FASTA	568	63,786
	10 20 30 40 50 60 MSASVFNRCW SKVILETLSR QGVSHFCIAP GSRSTPLTLE AIRLQENGRG TCHAHFDERS 70 80 90 100 110 120 LGFFALGIAK ASKKPVAVIV TSGTATANLY PAIIEARQTD VPLIILTADR PPELLECGAN 130 140 150 160 170 180 QAILQQNMFA QYPIASINLP RPSQNYSAQW LISVLDQACF RQKQGGVIHI NVPFAEPLYN 190 200 210 220 230 240 ANNDEIDLHP WLSNIQSWLT QNKNWIQHQE QHTEVITHKY WDQWRTKKGI IIVGRLPSEQ 250 260 270 280 290 300 AMGIAEWADN MGWIMITDIQ SHVKPTLPYA DIWLANQTVR KKLLQAEIVI QFGSGFIGKR 310 320 330 340 350 360 INQFLAEFKG EYWIIENNQK AVDPYHHAHT RFNAKPHHWL RAHPPMRKKP WLLEPLALAK 370 380 390 400 410 420 FCADFIKQRV GSNLNEASLA HNIELLLPKS NSVLFLGNSL FVRLADALSQ PSANYPIYTN 430 440 450 460 470 480 RGASGIDGLL ATAAGIAVGS EQTLVAMIGD TSTLYDLNSF ALFKQLNQPA IIFVINNNGG 490 500 510 520 530 540 AIFDMLPVDI AVKEKYYRMS HYLEFSHIAA MFDLKYARPY TWADLATVLK QAYSRRETTV 550 560 IEIKVNPNDG SNIYKDLIDK IGHALIGV

References

[1]

"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd." Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J. J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 129Pt.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000436 Genomic DNA. Translation: ABI24894.1.
RefSeq	YP_718829.1. NC_008309.1.
3D structure databases
ProteinModelPortal	Q0I316.
ModBase	Search...
Protein-protein interaction databases
STRING	205914.HS_0617.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABI24894; ABI24894; HS_0617.
GeneID	4240103.
KEGG	hso:HS_0617.
PATRIC	20281207. VBIHaeSom53361_0646.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1165.
HOGENOM	HOG000218360.
KO	K02551.
OMA	DGGGIFH.
ProtClustDB	PRK07449.
Enzyme and pathway databases
BioCyc	HSOM205914:GJ7V-644-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_HAES1

Accession

Primary (citable) accession number: Q0I316

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program