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UniProtKB - P23970 (MEND_BACSU)
Protein
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
Gene
menD
Organism
Bacillus subtilis (strain 168)
Status
Functioni
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).
UniRule annotationCaution
Used to include what was called 'MenCF'.Curated
Catalytic activityi
- 2-oxoglutarate + H+ + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2UniRule annotationEC:2.2.1.9UniRule annotation
Cofactori
Protein has several cofactor binding sites:- Mg2+UniRule annotation, Mn2+UniRule annotation
- thiamine diphosphateUniRule annotationNote: Binds 1 thiamine pyrophosphate per subunit.UniRule annotation
: 1,4-dihydroxy-2-naphthoate biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.
Pathwayi: menaquinone biosynthesis
This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotationView all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.
GO - Molecular functioni
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity Source: UniProtKB-UniRule
- magnesium ion binding Source: UniProtKB-UniRule
- manganese ion binding Source: UniProtKB-UniRule
- thiamine pyrophosphate binding Source: UniProtKB-UniRule
GO - Biological processi
- menaquinone biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Transferase |
Biological process | Menaquinone biosynthesis |
Ligand | Magnesium, Manganese, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyci | BSUB:BSU30820-MONOMER |
BRENDAi | 2.2.1.9, 658 |
SABIO-RKi | P23970 |
UniPathwayi | UPA00079 UPA01057;UER00164 |
Names & Taxonomyi
Protein namesi | Recommended name: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseUniRule annotation (EC:2.2.1.9UniRule annotation)Short name: SEPHCHC synthaseUniRule annotation Alternative name(s): Menaquinone biosynthesis protein MenDUniRule annotation |
Gene namesi | Name:menDUniRule annotation Ordered Locus Names:BSU30820 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000090828 | 1 – 580 | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseAdd BLAST | 580 |
Proteomic databases
PaxDbi | P23970 |
PRIDEi | P23970 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotationProtein-protein interaction databases
STRINGi | 224308.BSU30820 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P23970 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P23970 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1165, Bacteria |
InParanoidi | P23970 |
OMAi | RQKPWLL |
PhylomeDBi | P23970 |
Family and domain databases
HAMAPi | MF_01659, MenD, 1 hit |
InterProi | View protein in InterPro IPR029035, DHS-like_NAD/FAD-binding_dom IPR004433, MenaQ_synth_MenD IPR032264, MenD_middle IPR029061, THDP-binding IPR012001, Thiamin_PyroP_enz_TPP-bd_dom IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR42916, PTHR42916, 1 hit |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF16582, TPP_enzyme_M_2, 1 hit PF02776, TPP_enzyme_N, 1 hit |
PIRSFi | PIRSF004983, MenD, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00173, menD, 1 hit |
i Sequence
Sequence statusi: Complete.
P23970-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTVNPITHYI GSFIDEFALS GITDAVVCPG SRSTPLAVLC AAHPDISVHV
60 70 80 90 100
QIDERSAGFF ALGLAKAKQR PVLLICTSGT AAANFYPAVV EAHYSRVPII
110 120 130 140 150
VLTADRPHEL REVGAPQAIN QHFLFGNFVK FFTDSALPEE SPQMLRYIRT
160 170 180 190 200
LASRAAGEAQ KRPMGPVHVN VPLREPLMPD LSDEPFGRMR TGRHVSVKTG
210 220 230 240 250
TQSVDRESLS DVAEMLAEAE KGMIVCGELH SDADKENIIA LSKALQYPIL
260 270 280 290 300
ADPLSNLRNG VHDKSTVIDA YDSFLKDDEL KRKLRPDVVI RFGPMPVSKP
310 320 330 340 350
VFLWLKDDPT IQQIVIDEDG GWRDPTQASA HMIHCNASVF AEEIMAGLTA
360 370 380 390 400
ATRSSEWLEK WQFVNGRFRE HLQTISSEDV SFEGNLYRIL QHLVPENSSL
410 420 430 440 450
FVGNSMPIRD VDTFFEKQDR PFRIYSNRGA NGIDGVVSSA MGVCEGTKAP
460 470 480 490 500
VTLVIGDLSF YHDLNGLLAA KKLGIPLTVI LVNNDGGGIF SFLPQASEKT
510 520 530 540 550
HFEDLFGTPT GLDFKHAAAL YGGTYSCPAS WDEFKTAYAP QADKPGLHLI
560 570 580
EIKTDRQSRV QLHRDMLNEA VREVKKQWEL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 112 | E → R in AAA50398 (PubMed:8566759).Curated | 1 | |
Sequence conflicti | 112 | E → R in AAC37014 (PubMed:8566759).Curated | 1 | |
Sequence conflicti | 152 | A → P in AAC37014 (PubMed:8566759).Curated | 1 | |
Sequence conflicti | 540 – 580 | PQADK…KQWEL → RRQTSPDSI in AAA50399 (PubMed:8566759).CuratedAdd BLAST | 41 | |
Sequence conflicti | 540 – 580 | PQADK…KQWEL → RRQTSPDSI in AAC37014 (PubMed:8566759).CuratedAdd BLAST | 41 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M74521 Genomic DNA Translation: AAA50398.1 Sequence problems. M74521 Genomic DNA Translation: AAA50399.1 Sequence problems. M74538 Genomic DNA Translation: AAC37014.1 AF008220 Genomic DNA Translation: AAC00224.1 AL009126 Genomic DNA Translation: CAB15060.1 |
PIRi | G69656 |
RefSeqi | NP_390960.1, NC_000964.3 WP_003229050.1, NZ_JNCM01000036.1 |
Genome annotation databases
EnsemblBacteriai | CAB15060; CAB15060; BSU_30820 |
GeneIDi | 937198 |
KEGGi | bsu:BSU30820 |
PATRICi | fig|224308.179.peg.3340 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M74521 Genomic DNA Translation: AAA50398.1 Sequence problems. M74521 Genomic DNA Translation: AAA50399.1 Sequence problems. M74538 Genomic DNA Translation: AAC37014.1 AF008220 Genomic DNA Translation: AAC00224.1 AL009126 Genomic DNA Translation: CAB15060.1 |
PIRi | G69656 |
RefSeqi | NP_390960.1, NC_000964.3 WP_003229050.1, NZ_JNCM01000036.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2X7J | X-ray | 2.35 | A/B/C/D | 1-580 | [»] | |
SMRi | P23970 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU30820 |
Proteomic databases
PaxDbi | P23970 |
PRIDEi | P23970 |
Genome annotation databases
EnsemblBacteriai | CAB15060; CAB15060; BSU_30820 |
GeneIDi | 937198 |
KEGGi | bsu:BSU30820 |
PATRICi | fig|224308.179.peg.3340 |
Phylogenomic databases
eggNOGi | COG1165, Bacteria |
InParanoidi | P23970 |
OMAi | RQKPWLL |
PhylomeDBi | P23970 |
Enzyme and pathway databases
UniPathwayi | UPA00079 UPA01057;UER00164 |
BioCyci | BSUB:BSU30820-MONOMER |
BRENDAi | 2.2.1.9, 658 |
SABIO-RKi | P23970 |
Miscellaneous databases
EvolutionaryTracei | P23970 |
Family and domain databases
HAMAPi | MF_01659, MenD, 1 hit |
InterProi | View protein in InterPro IPR029035, DHS-like_NAD/FAD-binding_dom IPR004433, MenaQ_synth_MenD IPR032264, MenD_middle IPR029061, THDP-binding IPR012001, Thiamin_PyroP_enz_TPP-bd_dom IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR42916, PTHR42916, 1 hit |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF16582, TPP_enzyme_M_2, 1 hit PF02776, TPP_enzyme_N, 1 hit |
PIRSFi | PIRSF004983, MenD, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR00173, menD, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MEND_BACSU | |
Accessioni | P23970Primary (citable) accession number: P23970 Secondary accession number(s): O34492, P23969 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 1, 1992 |
Last sequence update: | July 15, 1999 | |
Last modified: | February 23, 2022 | |
This is version 147 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families