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Protein

Arginine decarboxylase

Gene

gCARADC8

Organism
Dianthus caryophyllus (Carnation) (Clove pink)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation
  • pyridoxal 5'-phosphateUniRule annotation

Pathwayi: agmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Arginine decarboxylase (ADC), Arginine decarboxylase (gCARADC8)
This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Biological processi

Spermidine biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
Gene namesi
Name:gCARADC8Imported
OrganismiDianthus caryophyllus (Carnation) (Clove pink)Imported
Taxonomic identifieri3570 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesCaryophyllaceaeCaryophylleaeDianthus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei156N6-(pyridoxal phosphate)lysineUniRule annotation1

Structurei

3D structure databases

ProteinModelPortaliO04429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 397Orn_Arg_deC_NInterPro annotationAdd BLAST265
Domaini493 – 603Orn_DAP_Arg_deCInterPro annotationAdd BLAST111

Sequence similaritiesi

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.UniRule annotation

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O04429-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAVACYVDT SAAVYGGAGA LSLPAPEINF SGVPPTTNST TVNQPPLPQQ
60 70 80 90 100
WSPSLSAELY RIDRWGPPYF AVNSSGNVTV KPFGDATLPH QEIDLLKVVK
110 120 130 140 150
KVSDPKSSSG LGLHLPVIIR FPDVLKHRLE SLQSAFDFAV RTHGYGSHYQ
160 170 180 190 200
GVYPVKCNQD RYIVEDIVEF GSGFRFGLEA GSKPELLMAM SSLCKGSPDS
210 220 230 240 250
LLVCNGFKDA EYISLAIIGR KLGLNTVIVI EQEEEVDMAI ELSRKMGIRP
260 270 280 290 300
VVGVRAKLRT KHSGHFGSTS GEKGKFGLTT TQILRVVRKL ESFGMLDCLQ
310 320 330 340 350
LLHFHIGSQI PTTALLSDGV AEASQVYCEL TRLGAHMRVI DIGGGLGIDY
360 370 380 390 400
DGSKSGDSDL SVGYTLEEYA SAVVGTVKSV CDRKGVKSPV ICSESGRAIV
410 420 430 440 450
SHHSILVFEA VSSSSSASPP MPGSTLALDY LVDGLTDEVK GEYRSLTAAA
460 470 480 490 500
MRGEYESCLM YSGMLKQRCV ELFKDGCLGM EQLAAVDGLC ELVSKALGVA
510 520 530 540 550
DGVCTYNVNL SVFTSIPDFW GIGQLFPIMP IHRLDQQPKA RGILSDLTCD
560 570 580 590 600
SDGKIDKFIG DESSLPLHEL SGGEGYYLGM FLGGAYEEAL GGVHNLFGGP
610 620 630 640 650
SVVRVQQSDG PQSYAVTRAV PGPSSSDVLR VMHHEPELMF QTLKHRAEEC
660 670 680 690 700
DNDYTAGPLA DMLAQSFNST PYLVPGHATG SCGLSNGSGL VNGCREYFYG
710 720
VDDGCNAAAV DAAAGEEEQW SYVCA
Length:725
Mass (Da):77,589
Last modified:July 1, 1997 - v1
Checksum:i701C3642511ABCF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF002017 Genomic DNA. Translation: AAB60880.1.
PIRiT10709.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF002017 Genomic DNA. Translation: AAB60880.1.
PIRiT10709.

3D structure databases

ProteinModelPortaliO04429.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiO04429_DIACA
AccessioniPrimary (citable) accession number: O04429
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 1997
Last sequence update: July 1, 1997
Last modified: October 5, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.