Carboxynorspermidine/carboxyspermidine decarboxylase - Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

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Q9KRL4 (NSPC_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Carboxynorspermidine/carboxyspermidine decarboxylase
Short name=CANS DC/CAS DC
Short name=CANSDC/CASDC
EC=4.1.1.-

Gene names

Name:	nspC
Ordered Locus Names:	VC_1623

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine. Essential for biofilm formation. Ref.2
Catalytic activity	Carboxynorspermidine = bis(3-aminopropyl)amine + CO₂. Carboxyspermidine = spermidine + CO₂.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Disruption phenotype	Abolishes sym-norspermidine and spermidine accumulation and results in substantially increased accumulation of diaminopropane, whereas putrescine levels remain unaffected. Disappearance of norspermidine and accumulation of carboxynorspermidine. 50-60% reduction in growth rate of planktonic cells and severely reduced biofilm formation, which can be rescued by exogenously supplied sym-norspermidine but not spermidine. Not required for colonizing the small intestine in infant mouse model of infection. Ref.2
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family. NspC subfamily.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Spermidine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nor-spermidine biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB single-species biofilm formation Inferred from direct assay Ref.2. Source: UniProtKB spermidine biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carboxy-lyase activity Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 387

387

Carboxynorspermidine/carboxyspermidine decarboxylase

PRO_0000420247

Sites

Binding site

248

Substrate By similarity

Binding site

284

Substrate By similarity

Amino acid modifications

Modified residue

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9KRL4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B75DE87C2BBC5C15
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FASTA

387

43,099

        10         20         30         40         50         60 
METLQDIGTN MLKDELRTPY FMIDEAKLIA NLEIAKHLKE ISGVKMVLAL KCFSTWGVFD 

        70         80         90        100        110        120 
IIKPYLDGTT SSGPFEVKLG YETFGGETHA YSVGYSEEDV KEVIDICDKM IFNSQSQLAA 

       130        140        150        160        170        180 
YRHLVEGKAS LGLRINPGVS YAGQDLANPA RQFSRLGVQA DHIDESVFDS INGVMFHMNC 

       190        200        210        220        230        240 
ENKDVDAFIG LLDAISERFG RYLDKLDWVS LGGGVFFTWP GYDVEKLGAA LKAFAERHAV 

       250        260        270        280        290        300 
QLYLEPGEAI ITKTTDLVVT VVDIVENGMK TAIVDSATEA HRLDTLIYKE PASVLEASDK 

       310        320        330        340        350        360 
GQHEYVIGSC SCLAGDQFCV AKFDEPLQVG QKLHILDSAG YTMVKLNWFN GLKMPSVYCE 

       370        380 
RKNGQIQKIN QFGYEDFKRT LSLWSIE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.
[2]	"An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae." Lee J., Sperandio V., Frantz D.E., Longgood J., Camilli A., Phillips M.A., Michael A.J. J. Biol. Chem. 284:9899-9907(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE. Strain: El Tor C6709 / Serotype O1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF94776.1.
PIR	H82176.
RefSeq	NP_231262.1. NC_002505.1.
3D structure databases
ProteinModelPortal	Q9KRL4.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VC1623.
Protocols and materials databases
DNASU	2613879.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF94776; AAF94776; VC_1623.
GeneID	2613879.
KEGG	vch:VC1623.
PATRIC	20082308. VBIVibCho83274_1550.
Phylogenomic databases
KO	K13747.
OMA	DCLEMPY.
ProtClustDB	CLSK870069.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15802.
Family and domain databases
Gene3D	2.40.37.10. 1 hit.
InterPro	IPR009006. Ala_racemase/Decarboxylase_C. IPR022643. De-COase2_C. IPR005730. Nsp_de-COase. [Graphical view]
Pfam	PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view]
PIRSF	PIRSF038941. NspC. 1 hit.
SUPFAM	SSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMs	TIGR01047. nspC. 1 hit.
PROSITE	PS00878. ODR_DC_2_1. False negative. PS00879. ODR_DC_2_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NSPC_VIBCH

Accession

Primary (citable) accession number: Q9KRL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents