Q3M3Y3 (MEND_ANAVT) 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:	Ava_4706

Organism

Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]

Taxonomic identifier

240292 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena › Anabaena variabilis

Protein attributes

Sequence length	583 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 ABA24303.1 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 – 583	583	2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase HAMAP-Rule MF_01659		PRO_0000341700

Sequences

	Sequence		Length	Mass (Da)
	Q3M3Y3 [UniParc]. Last modified July 1, 2008. Version 2. Checksum: 8F1C11A039C39BD9	FASTA	583	65,551
	10 20 30 40 50 60 MPIAYKNINQ LWAYVFTETL KRLGLAYAVI CPGSRSTPLA VAFAQQAPDI EGISILDERS 70 80 90 100 110 120 AAFFALGLAK ATNRPVAIVC TSGTAGANFY PAVIEAQESR VPLLLLTADR PPELRDCHSG 130 140 150 160 170 180 QTIDQVKLFG SYPNWQTELA LPVSDMGMLG YLRQTVIHSW YRMQAPTPGP VHLNIPFRDP 190 200 210 220 230 240 LAPIPDGADL SYLLTKFHPE EFFAGITDTT SLPDHSQLSI PPEWLKSQRG IIIAGVAQPQ 250 260 270 280 290 300 QPQEYCRAIA RLSQTLQWPV LAEGLSPIRN YADLNPYLIS TYDLILRNQQ LATRLAPDMV 310 320 330 340 350 360 IQIGDMPTSK ELRTWIDTHQ PRRWVIDPSD QNLDPLHGRT THLRIRVEEL GCKGVEEDKS 370 380 390 400 410 420 SVSEYLQLWC NAETKVRVNV DETLDKMEDL VECKAAWLLS QILPPETPLF IANSMPVRDV 430 440 450 460 470 480 EFFWKPNNLR VRSHFNRGAN GIDGTLSTAL GIAHRHQSSV LITGDLALLH DTNGFLIRNK 490 500 510 520 530 540 FVGHLTIILI NNNGGGIFEM LPIAKFEPPF EEFFGTPQDI DFAQLCTTYN VQHELIHSWV 550 560 570 580 HLQQRLNPLP NTGIRVLELR TNRKIDAQWR RDNLSNFAAD NII

References

[1]

"Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000117 Genomic DNA. Translation: ABA24303.1. Different initiation.
RefSeq	YP_325198.1. NC_007413.1.
3D structure databases
ProteinModelPortal	Q3M3Y3.
ModBase	Search...
Protein-protein interaction databases
STRING	240292.Ava_4706.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABA24303; ABA24303; Ava_4706.
GeneID	3679725.
KEGG	ava:Ava_4706.
PATRIC	35430897. VBIAnaVar43351_5969.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1165.
HOGENOM	HOG000218359.
KO	K02551.
ProtClustDB	PRK07449.
Enzyme and pathway databases
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_ANAVT

Accession

Primary (citable) accession number: Q3M3Y3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	July 1, 2008
Last modified:	May 1, 2013
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program