Q55725 (MEND_SYNY3) 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:	sll0603

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	595 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 Reference 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 – 595	595	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659		PRO_0000341878

Sequences

	Sequence		Length	Mass (Da)
	Q55725 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 62CF0EA48B20D87E	FASTA	595	66,133
	10 20 30 40 50 60 MVDFTNPNTL AASVLVETLF RLGLQQAVIC PGSRSSPLTV ALARHGGIDC VVSLDERSAS 70 80 90 100 110 120 FFALGHGKRT GQPVALVCTS GTAAANFLPA IIEAHYSQVP LLVLTGDRPP RLRHCRAGQT 130 140 150 160 170 180 IDQTKLYGHY PQWQTELALP EPNMDYCHYL RQTALHSWQK CFWPGLGVVH LNCPFDEPLV 190 200 210 220 230 240 PLEHARESLQ HLAEEFSKEH FYRGLTTFTT MNRGEAISLP VNFSIFSFPS PQLDFSPLGL 250 260 270 280 290 300 ILVGVMPGGE TPSLLTDILA IARGLGYPVL CDALCSLRNY DDGQTALITN YDFLIRCPRW 310 320 330 340 350 360 AEQLVPEQII QIGELPTSKA LRHWLGTIDC PRYILNFHGE NLDPLQGQTI YLSASVAQVA 370 380 390 400 410 420 EYIHNQGFIP DAEQKNYAHS WLEKQRQSQT IIISALADAH TPLMVAQLAH CLPPQTNLFV 430 440 450 460 470 480 ANSLPVRWLE FFWPANGDHH RIFVNRGANG IDGTLSTAMG IAHRSRGETV LLTGDLSLLH 490 500 510 520 530 540 DSNGFLNQSQ MRGNLTIILL NNNGGGIFQT LPIAQCEDVF ETYFATPQGV DFGQLCRTYG 550 560 570 580 590 VEHKIITNLW DLKEQWPSNN SSPIRVLEII GDRHQEAQWL KSLQAQFCCA DSLIQ

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA10366.1.
PIR	S76520.
RefSeq	NP_442296.1. NC_000911.1. YP_005652356.1. NC_017277.1. YP_007452172.1. NC_020286.1.
3D structure databases
ProteinModelPortal	Q55725.
ModBase	Search...
Protein-protein interaction databases
STRING	1148.sll0603.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA10366; BAA10366; BAA10366.
GeneID	12253576. 14617850. 952514.
KEGG	syn:sll0603. syy:SYNGTS_2403.
PATRIC	23842248. VBISynSp132158_2664.
Phylogenomic databases
eggNOG	COG1165.
HOGENOM	HOG000218359.
KO	K02551.
OMA	DGGGIFH.
ProtClustDB	PRK07449.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13897.
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_SYNY3

Accession

Primary (citable) accession number: Q55725

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program