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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

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

GO - Molecular functioni

  1. arginine decarboxylase activity Source: TIGR
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. polyamine biosynthetic process Source: TIGR
  3. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
Short name:
ADCUniRule annotation
Gene namesi
Name:speAUniRule annotation
Ordered Locus Names:VC_A0815
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Biosynthetic arginine decarboxylasePRO_0000149983Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi243277.VCA0815.

Structurei

3D structure databases

ProteinModelPortaliQ9KLD1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 30011Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
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.
SUPFAMiSSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9KLD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYDVEQPSK LDRVRADYNV HYWSQGFFGI DDQGEVYVSP RKDKAHQTQL
60 70 80 90 100
SSIVKQLEAR DLNLPVLVRF PQILHQRVHN ICDAFNQAIE EYDYPNKYLL
110 120 130 140 150
VYPIKVNQQK EVVDEILASQ AELEHKQLGL EAGSKPELLA VLAMAQQASS
160 170 180 190 200
VIVCNGYKDR EYIRLALIGE KLGHKVFIVL EKLSELDLVL KEAKSLGVKP
210 220 230 240 250
RLGLRIRLAS QGAGKWQSSG GEKSKFGLAA SQVLTVINRL KAENQLEALQ
260 270 280 290 300
LVHFHLGSQM ANIRDVRNGV NEAVRFYCEL RELGAHIDFF DVGGGLAVDY
310 320 330 340 350
DGTRSQSSNS MNYGLHEYAR NIVSTVSDVC NLYGQPRPVI ISESGRSITA
360 370 380 390 400
HHAVLITNVI GTEAYSPEEI PAPGADAPML LKNMWRGFEE VQHGTDDRAL
410 420 430 440 450
IEIYNDTQSD LSEAHSQFAT GVLNLEHRAW AEQLSLRIYH ELRQKMSNKN
460 470 480 490 500
RFHRPILDEL QERLADKFFV NFSLFQSLPD AWGIDQVFPV LPLSGLEEMN
510 520 530 540 550
DRRAVMLDIT CDSDGAVEQY VEGQGIESTL PVPAWTSDKP YLMGFFLVGA
560 570 580 590 600
YQEILGDMHN LFGDTHSAVV NINDNGESEI AFINEGDTVE DMMRYVHIDV
610 620 630 640
DKIRTNYRQL VSQRVAKEEQ ETVLAELELG LSGYTYLEDF
Length:640
Mass (Da):72,249
Last modified:March 29, 2004 - v2
Checksum:i851D1CE7D6E466F9
GO

Sequence cautioni

The sequence AAF96713.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003853 Genomic DNA. Translation: AAF96713.1. Different initiation.
PIRiE82414.
RefSeqiNP_233201.1. NC_002506.1.

Genome annotation databases

EnsemblBacteriaiAAF96713; AAF96713; VC_A0815.
GeneIDi2611850.
KEGGivch:VCA0815.
PATRICi20086176. VBIVibCho83274_3435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003853 Genomic DNA. Translation: AAF96713.1. Different initiation.
PIRiE82414.
RefSeqiNP_233201.1. NC_002506.1.

3D structure databases

ProteinModelPortaliQ9KLD1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VCA0815.

Protocols and materials databases

DNASUi2611850.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF96713; AAF96713; VC_A0815.
GeneIDi2611850.
KEGGivch:VCA0815.
PATRICi20086176. VBIVibCho83274_3435.

Phylogenomic databases

eggNOGiCOG1166.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
InterProiIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view]
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.
SUPFAMiSSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiSPEA_VIBCH
AccessioniPrimary (citable) accession number: Q9KLD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: January 7, 2015
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.