NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 8185 / IAM 1031 / IFO 3331 / NCDO 717 / NCIB 8598;
DOI=10.1074/jbc.M309658200; PubMed=14670971 [NCBI, ExPASy, EBI, Israel, Japan]
Kessler N., Schuhmann H., Morneweg S., Linne U., Marahiel M.A.;
"The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 57 catalytic domains.";
J. Biol. Chem. 279:7413-7419(2004).

[2]

CHARACTERIZATION.
STRAIN=ATCC 8185 / IAM 1031 / IFO 3331 / NCDO 717 / NCIB 8598;
DOI=10.1021/bi050074t; PubMed=15938641 [NCBI, ExPASy, EBI, Israel, Japan]
Schracke N., Linne U., Mahlert C., Marahiel M.A.;
"Synthesis of linear gramicidin requires the cooperation of two independent reductases.";
Biochemistry 44:8507-8513(2005).

Comments

FUNCTION: In the final step of gramicidin biosynthesis, reduces the pentadecapeptide-aldehyde intermediate, that is released from the terminal module of the non-ribosomal peptide synthetase lgrD, to the final product ethanolamine-containing gramicidin.
PATHWAY: Antibiotic biosynthesis; gramicidin S biosynthesis .
MISCELLANEOUS: The reduction is strictly NADPH-dependent.
MISCELLANEOUS: Linear gramicidine is a pentadecapeptide antibiotic produced during sporulation.
SIMILARITY: Belongs to the thioesterase family.
CAUTION: Although this protein is said to have a reductase activity, it clearly belongs to the thioesterase (hydrolase) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ566197; CAD92848.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q70LM8.

Ontologies

GO:0016788;	Molecular function: hydrolase activity, acting on ester bonds (inferred from electronic annotation from InterPro).
GO:0016491;	Molecular function: oxidoreductase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0017000;	Biological process: antibiotic biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR012223; TEII.
IPR001031; Thioesterase.
Graphical view of domain structure.

PANTHER

PTHR11487; TEII; 1.

Pfam

PF00975; Thioesterase; 1.
Pfam graphical view of domain structure.

Other

ProtoNet

Q70LM8.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antibiotic biosynthesis; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 263`	`263`	`Linear gramicidin dehydrogenase lgrE.`	`PRO_0000180363`
`ACT_SITE`	`96 96`		`By similarity.`

Sequence information

Length: 263 AA [This is the length of the unprocessed precursor]

Molecular weight: 30103 Da [This is the MW of the unprocessed precursor]

CRC64: 885DE9A45B041641 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQKTHVSPSR WLLSPKMTAE AEVLLFSFHY AGGHAGIYRE WQKKLPVQIG VCPVQLPGRS 

        70         80         90        100        110        120 
NRFMEPYYTD LSVMIRELAE ALLPHLNRPF AFFGHSMGAL VSFELARYLR NQYGIKPRHM 

       130        140        150        160        170        180 
FASGRHAPHL PDPGEAIHHL PDAEFLKGLR TLNGTPKELF ENEENEEILQ MLLPMLRADF 

       190        200        210        220        230        240 
TICEQYQYQE EEPLGCGLTA IGGWQDPDIT VAHMEAWRKH TSASFQMHML QGDHFFLHSE 

       250        260 
QEQLLAIIES TLQSYLVGYR GIG

Q70LM8 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools