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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotationSAAS annotation

Cofactori

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

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

DecarboxylaseUniRule annotation, Lyase

Keywords - Biological processi

Polyamine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotation, Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1679-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotationSAAS annotation)
Short name:
ADCUniRule annotation
Gene namesi
Name:speAUniRule annotation
Ordered Locus Names:TTHA1640Imported
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)Imported
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1640.

Structurei

3D structure databases

ProteinModelPortaliQ5SHU0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.
PhylomeDBiQ5SHU0.

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.
IPR022653. De-COase2_pyr-phos_BS.
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.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SHU0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKRFTLKDA EELYLVPHWS GGFFRVGEKG DLEVTPLGPK GPAASLLEIV
60 70 80 90 100
EALRDEGRPL PLVLRFPQIL EARVRDLNEA FLEAMAKYGY QGTYRGVYPV
110 120 130 140 150
KVNQRRLVLE TVARAGRPYH LGLEAGSKPE LALILAQDLS EEALITTNGF
160 170 180 190 200
KDDDFVRLAL MGRKLGRNVV ITLEKFAELF RVLRLSKELG VKPLLGIRYK
210 220 230 240 250
LKAKGAGQWE ASGGENAKFG LTTPEIVRAV EVLQEEGLLD ALVMLHAHIG
260 270 280 290 300
SQVTDIRRIK AAVREAAQTY VQLRKLGAPL RYLNLGGGLA VDYDGSKTNF
310 320 330 340 350
YASANYTLSE YAENLVYVTK EVVEAQGEPH PILVTESGRA ITAYHEVLVL
360 370 380 390 400
QVIDVIAPPG EARPSPPPPE AHPLVKELWE SLQSLSPKNF QEVYHDAFAD
410 420 430 440 450
KETLQTLYDL GLVSLRDRAL AEEIFYHIAR RVQTIAQNLP YVPDELEDLE
460 470 480 490 500
KLLADKLVCN FSVFQSLPDA WAIHQLFPVV PLSRLLEPPT RRATLVDISC
510 520 530 540 550
DSDGKMDRFI DLHDVRQTLP VHPVRPGEPY YLGVFLVGAY QDVLGSNHNL
560 570 580 590 600
FGQVGEAHVR VEEEGFAIER FVGGETAERV IEKMGFTARE LMLGVERLVR
610 620
QSRLSPVEKG AFLERYAREL QGYTYLED
Length:628
Mass (Da):70,241
Last modified:December 21, 2004 - v1
Checksum:i565F8577FDF8D999
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71463.1.
RefSeqiYP_144906.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71463; BAD71463; BAD71463.
GeneIDi3169310.
KEGGittj:TTHA1640.
PATRICi23958235. VBITheThe93045_1610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71463.1.
RefSeqiYP_144906.1. NC_006461.1.

3D structure databases

ProteinModelPortaliQ5SHU0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1640.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71463; BAD71463; BAD71463.
GeneIDi3169310.
KEGGittj:TTHA1640.
PATRICi23958235. VBITheThe93045_1610.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.
PhylomeDBiQ5SHU0.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciTTHE300852:GH8R-1679-MONOMER.

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.
IPR022653. De-COase2_pyr-phos_BS.
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.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579Imported.

Entry informationi

Entry nameiQ5SHU0_THET8
AccessioniPrimary (citable) accession number: Q5SHU0
Entry historyi
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: February 4, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.