(data stored in SCRATCH zone)

SWISSPROT: Q5LVU5_RUEPO

ID   Q5LVU5_RUEPO            Unreviewed;       389 AA.
AC   Q5LVU5;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 2.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000256|PIRNR:PIRNR038941};
DE            Short=CANS DC/CAS DC {ECO:0000256|PIRNR:PIRNR038941};
DE            Short=CANSDC/CASDC {ECO:0000256|PIRNR:PIRNR038941};
DE            EC=4.1.1.96 {ECO:0000256|PIRNR:PIRNR038941};
GN   Name=nspC {ECO:0000313|EMBL:AAV93915.2};
GN   OrderedLocusNames=SPO0600 {ECO:0000313|EMBL:AAV93915.2};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93915.2, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93915.2, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93915.2, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine
CC       and carboxyspermidine. {ECO:0000256|PIRNR:PIRNR038941}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carboxynorspermidine + H(+) = CO2 + norspermidine;
CC         Xref=Rhea:RHEA:34099, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57920, ChEBI:CHEBI:65070; EC=4.1.1.96;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038941};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carboxyspermidine + H(+) = CO2 + spermidine;
CC         Xref=Rhea:RHEA:34095, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57834, ChEBI:CHEBI:65072; EC=4.1.1.96;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038941};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038941,
CC         ECO:0000256|SAAS:SAAS00373528};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR038941}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038941}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. NspC subfamily. {ECO:0000256|PIRNR:PIRNR038941}.
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DR   EMBL; CP000031; AAV93915.2; -; Genomic_DNA.
DR   RefSeq; WP_030003177.1; NC_003911.12.
DR   STRING; 246200.SPO0600; -.
DR   EnsemblBacteria; AAV93915; AAV93915; SPO0600.
DR   KEGG; sil:SPO0600; -.
DR   eggNOG; ENOG4105D3D; Bacteria.
DR   eggNOG; COG0019; LUCA.
DR   HOGENOM; HOG000005225; -.
DR   KO; K13747; -.
DR   OMA; YTMVKTT; -.
DR   OrthoDB; 861683at2; -.
DR   BioCyc; RPOM246200:G1G48-608-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045312; P:nor-spermidine biosynthetic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06829; PLPDE_III_CANSDC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR005730; Nsp_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43727:SF1; PTHR43727:SF1; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PIRSF; PIRSF038941; NspC; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01047; nspC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LVU5.
DR   SWISS-2DPAGE; Q5LVU5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR038941};
KW   Decarboxylase {ECO:0000256|PIRNR:PIRNR038941};
KW   Lyase {ECO:0000256|PIRNR:PIRNR038941};
KW   Polyamine biosynthesis {ECO:0000256|PIRNR:PIRNR038941};
KW   Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR038941,
KW   ECO:0000256|SAAS:SAAS00272807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Spermidine biosynthesis {ECO:0000256|PIRNR:PIRNR038941}.
FT   DOMAIN      108    343       Orn_DAP_Arg_deC. {ECO:0000259|Pfam:
FT                                PF00278}.
FT   BINDING     255    255       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR038941-1}.
FT   BINDING     291    291       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR038941-1}.
SQ   SEQUENCE   389 AA;  42700 MW;  2EEC6793A32BFF5C CRC64;
     MADVMQTQAG DAGAFRHFDL SRVPTPCFVV DEVAIERNLK ILRDISDRSG AHVLSALKAF
     SMFTLAPLVR QYLGGTCASG IYEARLGREE YGGEVATFCA GYKEQDIDEI LSLSNHIIFN
     SPAQKDRFLS RAQAAGVQVG LRINPEHSEG EIAKYDPCAP CSRLGTPVSL LTPETLKGVD
     GLHMHTLCEQ GFEPLLRTWA AVEPKLAPYL PGLKWLNFGG GHHITRADYD RDALIDFLKS
     LRARHGLDVY LEPGEAVALD AGILVGEILD LPSNGMDLAI TDISATCHMP DVIEAPYRPA
     LMDEADSGHT YRLGGPSCLA GDVIGDYTWD QPLTIGQRFA FLDQAHYSMV KTNTFNGVPL
     PTIALWNSKT DALRIVRQFD YSDFKDRLS
//

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