Skip Header

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

Q4L547

- MEND_STAHJ

UniProt

Q4L547 - MEND_STAHJ

(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

Organism
Staphylococcus haemolyticus (strain JCSC1435)
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).UniRule annotation

Catalytic activityi

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

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

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

BioCyciSHAE279808:GJX7-1974-MONOMER.
UniPathwayiUPA00079.
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:SH1919
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5565562-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthasePRO_0000341865Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH1919.

Structurei

3D structure databases

ProteinModelPortaliQ4L547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TPP enzyme family. MenD subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1165.
HOGENOMiHOG000218359.
KOiK02551.
OMAiQKPWLLE.
OrthoDBiEOG6NWBQW.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01659. MenD.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PIRSFiPIRSF004983. MenD. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00173. menD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q4L547-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNHNEALTKQ VYTFASELYA YGVREVVISP GSRSTPLAIA FEAHPNIKTW
60 70 80 90 100
IHPDERSAAF FALGLIKGSE RPVAILCTSG TAAANYTPAI AESQISRIPL
110 120 130 140 150
IVLTSDRPHE LRSVGAPQAI NQVNMFANYV NFQFDMPVAD GTDYMLDAIY
160 170 180 190 200
YQMQIASQYL YGPHRGPIHF NLPFREPLTP NLERQEWLTS YSKKLPHYQK
210 220 230 240 250
NINVQDIRHI LKEKKGLIIV GDMQHQAIDQ ILTYATVHDI PILADPLSQL
260 270 280 290 300
RKYNHPNVIT TYDLYYRAGL DIDVDFVIRV GKPVISKKLN QWLKRTNAYQ
310 320 330 340 350
ILVQNNDKID VFPTPPSISY EISANDFFRN LIEEAAVDRK DWINMWRTLE
360 370 380 390 400
SQARNTIDKH MTNATDEAAF VKILIDKLTK DDAIFVSNSM PVRDIDNLLY
410 420 430 440 450
NSEVEVYANR GANGIDGVVS TAIGMAVHKK ITLIIGDLAF YHDMNGLLMA
460 470 480 490 500
KINNINLNIV LLNNDGGGIF SYLPQKASAE AYFERLFGTP TGLNFEYTAL
510 520 530 540 550
LYDFTFKRFN TVADFTQEKL SHVNSHIYEM VTNRDDNMSQ HQILYKKLSG

ILNVTL
Length:556
Mass (Da):63,095
Last modified:August 2, 2005 - v1
Checksum:iFE88BE461C5A72D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05228.1.
RefSeqiYP_253834.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05228; BAE05228; SH1919.
GeneIDi3482100.
KEGGisha:SH1919.
PATRICi19619943. VBIStaHae67511_1894.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05228.1 .
RefSeqi YP_253834.1. NC_007168.1.

3D structure databases

ProteinModelPortali Q4L547.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279808.SH1919.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE05228 ; BAE05228 ; SH1919 .
GeneIDi 3482100.
KEGGi sha:SH1919.
PATRICi 19619943. VBIStaHae67511_1894.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00079 .
UPA01057 ; UER00164 .
BioCyci SHAE279808:GJX7-1974-MONOMER.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
HAMAPi MF_01659. MenD.
InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR004433. MenaQ_synth_MenD.
IPR029061. THDP-binding.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR011766. TPP_enzyme-bd_C.
[Graphical view ]
Pfami PF02775. TPP_enzyme_C. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF004983. MenD. 1 hit.
SUPFAMi SSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00173. menD. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiMEND_STAHJ
AccessioniPrimary (citable) accession number: Q4L547
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: August 2, 2005
Last modified: November 26, 2014
This is version 70 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