NSPC_VIBAL
ID NSPC_VIBAL Reviewed; 377 AA.
AC Q56575;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000303|PubMed:7812450, ECO:0000303|Ref.2, ECO:0000312|EMBL:BAA06561.1};
DE Short=CANS DC/CAS DC {ECO:0000303|PubMed:7812450};
DE Short=CANSDC/CASDC {ECO:0000250|UniProtKB:A8FNH9};
DE EC=4.1.1.96 {ECO:0000269|PubMed:1955861, ECO:0000269|PubMed:7812450, ECO:0000269|Ref.2};
DE AltName: Full=C-NSPD decarboxylase {ECO:0000303|Ref.2};
GN Name=nspC {ECO:0000312|EMBL:BAA06561.1};
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=ATCC 17749 / DSM 2171 / NBRC 15630 / NCIMB 1903 / XII-53;
RX PubMed=7812450; DOI=10.1099/13500872-140-11-3117;
RA Yamamoto S., Sugahara T., Tougou K., Shinoda S.;
RT "Cloning and nucleotide sequence of the carboxynorspermidine decarboxylase
RT gene from Vibrio alginolyticus.";
RL Microbiology 140:3117-3124(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 17749 / DSM 2171 / NBRC 15630 / NCIMB 1903 / XII-53;
RA Nakao H., Shinoda S., Yamamoto S.;
RT "Purification and properties of carboxynorspermidine decarboxylase, a novel
RT enzyme involved in norspermidine biosynthesis, from Vibrio alginolyticus.";
RL J. Gen. Microbiol. 136:1699-1704(1990).
RN [3]
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 17749 {ECO:0000269|PubMed:1955861};
RX PubMed=1955861; DOI=10.1099/00221287-137-7-1737;
RA Nakao H., Shinoda S., Yamamoto S.;
RT "Purification and some properties of carboxynorspermidine synthase
RT participating in a novel biosynthetic pathway for norspermidine in Vibrio
RT alginolyticus.";
RL J. Gen. Microbiol. 137:1737-1742(1991).
CC -!- FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and
CC carboxyspermidine. 2,3-diaminopropionic acid, 2,4-diaminobutyric acid,
CC L-ornithine or L-lysine cannot serve as substrates.
CC {ECO:0000269|Ref.2}.
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:0000269|PubMed:1955861, ECO:0000269|PubMed:7812450,
CC ECO:0000269|Ref.2};
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:0000269|PubMed:1955861, ECO:0000269|PubMed:7812450,
CC ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Dithiothreitol greatly stimulates activity,
CC maximum stimulation being at 5-20 mM dithiothreitol concentration.
CC Fe(3+), Fe(2+) and Mn(2+) severely inhibit activity (88%, 82% and 50%,
CC respectively), whereas Zn(2+) has a slightly inhibitory effect (23%)
CC and Mg(2+), Ca(2+), Cu(2+) and Cu(+) have no effect.
CC {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=175 uM for carboxynorspermidine (at 37 degrees Celsius and pH
CC 8.25) {ECO:0000269|Ref.2};
CC KM=4.8 uM for pyridoxal 5'-phosphate (at 37 degrees Celsius and pH
CC 8.25) {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 8.25. Stable at pH 7.5 and 4 degrees Celsius in the
CC presence of DTT, EDTA and NaN(3) for at least one month. 57% and 72%
CC of the maximum activity observed at pH 7.5 and 9.0, respectively.
CC {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. 75% and 51% of the maximum
CC activity remains at 30 and 45 degrees Celsius, respectively, but the
CC activity decreases rapidly at temperatures above 55 or below 20
CC degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC NspC subfamily. {ECO:0000255}.
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DR EMBL; D31783; BAA06561.1; -; Genomic_DNA.
DR AlphaFoldDB; Q56575; -.
DR SMR; Q56575; -.
DR STRING; 663.BAU10_08865; -.
DR eggNOG; COG0019; Bacteria.
DR BioCyc; MetaCyc:MON-13927; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR GO; GO:0045312; P:nor-spermidine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Decarboxylase; Direct protein sequencing; Lyase;
KW Polyamine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..377
FT /note="Carboxynorspermidine/carboxyspermidine
FT decarboxylase"
FT /id="PRO_0000420245"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT MOD_RES 41
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT CONFLICT 12
FT /note="S -> M (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42045 MW; 90C885DCC47BCDC3 CRC64;
MQQNELKTPY FSINEDKLIE NLEKAKQLKD ISGVKLVLAL KCFSTWGVFD IIKPYLDGTT
SSGPFEVKLG YETFGGETHA YSVGYSEDDV RDVADICDKM IFNSQSQLAA YRHIVEGKAS
IGLRLNPGVS YAGQDLANPA RQFSRLGVQA DHIKPEIFDG IDGVMFHMNC ENKDVDAFIG
LLDAISAQFG EYLDKLDWVS MGGGVFFTWP GYDIEKLGLA LKAFAEKHGV QMYLEPGERI
ITKTTDLVVT VVDIVENVKK TAIVDSATEA HRLDTLIYNE PASILEASEN GEHEYVIGSC
SCLAGDQFCV ANFEQPLEIG QRLHILDSAG YTMVKLNWFN GLRMPSVYCE RSNGDIQKLN
EFDYSDFKRS LSQWSVI
