SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A1UAX3

- MEND_MYCSK

UniProt

A1UAX3 - MEND_MYCSK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
Gene
menD, Mkms_0765
Organism
Mycobacterium sp. (strain KMS)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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) By similarity.UniRule annotation

Catalytic activityi

Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2.UniRule annotation

Cofactori

Magnesium or manganese By similarity.UniRule annotation
Binds 1 thiamine pyrophosphate per subunit By similarity.

Pathwayi

GO - Molecular functioni

  1. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. thiamine pyrophosphate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. menaquinone biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Menaquinone biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMSP189918:GH4X-769-MONOMER.
UniPathwayiUPA00079; UER00164.

Names & Taxonomyi

Protein namesi
Recommended name:
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (EC:2.2.1.9)
Short name:
SEPHCHC synthase
Alternative name(s):
Menaquinone biosynthesis protein MenD
Gene namesi
Name:menD
Ordered Locus Names:Mkms_0765
OrganismiMycobacterium sp. (strain KMS)
Taxonomic identifieri189918 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000638: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5475472-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthaseUniRule annotation
PRO_0000341782Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi189918.Mkms_0765.

Structurei

3D structure databases

ProteinModelPortaliA1UAX3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1165.
HOGENOMiHOG000218359.
KOiK02551.
OMAiWRSAVCR.
OrthoDBiEOG6NWBQW.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01659. MenD.
InterProiIPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
[Graphical view]
PfamiPF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF004983. MenD. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00173. menD. 1 hit.

Sequencei

Sequence statusi: Complete.

A1UAX3-1 [UniParc]FASTAAdd to Basket

« Hide

MNPSTAQARV VVDELVRGGV HDVVLCPGSR NAPLAFALAD ADRAGRLRLH    50
VRIDERTAGF LAIGLAVADR APVCVAMTSG TAVANLGPAV VEANYARVPL 100
IVLSANRPYE LLGTGANQTF EQLGYFGNQV RANISLGLAP ELSSGSPGDM 150
TSLNAQWRSA TCRVVVAATG SRSANAGPVQ FDIPLREPLV PTFDDDGSCP 200
PGRPDGKPWT HTPPVTFDQP LDIDLTPDTV VIAGHGAGVH PNLADLPTVA 250
EPTAPPAANP LHPMALRLLR PKQVIMLGRP TLHRPVSALL ADPSVPVYAL 300
TTGPRWPDVS GNSQATGTRA VTSGTPDPAW LRRCKEVNDH AVAAVREQLA 350
AHPLTTGLHV AAAVADAVRP GDQLVLGASN PVRDAALVGF TPHGVQVRSN 400
RGVAGIDGTV STAIGAALAH DRTGGRTIAL MGDLTFVHDS SGLLIGPTEP 450
TPRNLTIVVS NDNGGGIFEL LEQGDPRFSD VSSRVFGTPH DVDVGALCRA 500
YHVDNRQIEV GQLADALDEP HEGMRVLEVK ADRSSLRALH ASIKAAL 547
Length:547
Mass (Da):57,160
Last modified:February 6, 2007 - v1
Checksum:i95627771DCCEF164
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000518 Genomic DNA. Translation: ABL89981.1.
RefSeqiYP_936771.1. NC_008705.1.

Genome annotation databases

EnsemblBacteriaiABL89981; ABL89981; Mkms_0765.
GeneIDi4614965.
KEGGimkm:Mkms_0765.
PATRICi18100488. VBIMycSp70743_1295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000518 Genomic DNA. Translation: ABL89981.1 .
RefSeqi YP_936771.1. NC_008705.1.

3D structure databases

ProteinModelPortali A1UAX3.
ModBasei Search...

Protein-protein interaction databases

STRINGi 189918.Mkms_0765.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL89981 ; ABL89981 ; Mkms_0765 .
GeneIDi 4614965.
KEGGi mkm:Mkms_0765.
PATRICi 18100488. VBIMycSp70743_1295.

Phylogenomic databases

eggNOGi COG1165.
HOGENOMi HOG000218359.
KOi K02551.
OMAi WRSAVCR.
OrthoDBi EOG6NWBQW.

Enzyme and pathway databases

UniPathwayi UPA00079 ; UER00164 .
BioCyci MSP189918:GH4X-769-MONOMER.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
HAMAPi MF_01659. MenD.
InterProi IPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
[Graphical view ]
Pfami PF02776. TPP_enzyme_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF004983. MenD. 1 hit.
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00173. menD. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KMS.

Entry informationi

Entry nameiMEND_MYCSK
AccessioniPrimary (citable) accession number: A1UAX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi