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A4SPD6

- SPEA_AERS4

UniProt

A4SPD6 - SPEA_AERS4

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Aeromonas salmonicida (strain A449)
Status
Reviewed - 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

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

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciASAL382245:GJJN-2729-MONOMER.
UniPathwayiUPA00186; UER00284.

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:ASA_2740
OrganismiAeromonas salmonicida (strain A449)
Taxonomic identifieri382245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
ProteomesiUP000000225: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Biosynthetic arginine decarboxylasePRO_1000024252Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi382245.ASA_2740.

Structurei

3D structure databases

ProteinModelPortaliA4SPD6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni284 – 29411Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
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.
IPR022657. De-COase2_CS.
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.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4SPD6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNWSSKDSL KVYNVPYWGA GFFNINDAGH VTVAPDKSRP DAHIVISDAI
60 70 80 90 100
EQLRQSGLTT PVLLRFPDIL KSRVDALFNA FGQAIEKSGY EGDYLCVYPI
110 120 130 140 150
KVNQQSRVIE TISQSYSDKP RLGLEAGSKP ELLAVLSHHH EQGSVIVCNG
160 170 180 190 200
YKDREYIRHA LLGNLMGHKV YIVVEKPSEL EMVLDESARL NIKPNIGVRA
210 220 230 240 250
KLASTGSGMW ESSGGSMSKF GLSASQILAL VERLRSLDKL DCLQLLHFHL
260 270 280 290 300
GSQIANIRDI QGGIRECGRF YSELRRLGVP IDVVDVGGGL GVDYEGTRSQ
310 320 330 340 350
SHCSANYSLS EYANNVVWGI GDVCREFDLP YPTIISESGR ALTAHHAVLV
360 370 380 390 400
TNLIGAEGVE MSDISAPDED APTLLQNMWQ GWLDLRGEDP SLLEIFHDSV
410 420 430 440 450
ADLGDVNTQY TMGLLNLEQR AWAEMLHQNT CLALKEMLNP VNRNHRALAD
460 470 480 490 500
ELSEKLADKC FANFSLFQSL PDAWGIGQVF PVMPLTGLDR PLSRRGILMD
510 520 530 540 550
ITCDSDGQVE HYVDGLGVES TLPMPQYEEN EVCYVGFFLV GAYQEILGDL
560 570 580 590 600
HNLFGDTHCA EVCLDEEGKM DIRNVVRGDT VDQLLRYVNI DPSVIRENYQ
610 620 630
RIVSHPALDD ATRKALLDEL ELGLQGYAYL EDE
Length:633
Mass (Da):70,262
Last modified:May 15, 2007 - v1
Checksum:i75DA089696A72486
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000644 Genomic DNA. Translation: ABO90758.1.
RefSeqiWP_005309971.1. NC_009348.1.
YP_001142506.1. NC_009348.1.

Genome annotation databases

EnsemblBacteriaiABO90758; ABO90758; ASA_2740.
GeneIDi4995209.
KEGGiasa:ASA_2740.
PATRICi20791877. VBIAerSal2987_2714.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000644 Genomic DNA. Translation: ABO90758.1 .
RefSeqi WP_005309971.1. NC_009348.1.
YP_001142506.1. NC_009348.1.

3D structure databases

ProteinModelPortali A4SPD6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 382245.ASA_2740.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO90758 ; ABO90758 ; ASA_2740 .
GeneIDi 4995209.
KEGGi asa:ASA_2740.
PATRICi 20791877. VBIAerSal2987_2714.

Phylogenomic databases

eggNOGi COG1166.
HOGENOMi HOG000029191.
KOi K01585.
OMAi IDHYVDG.
OrthoDBi EOG676Z0R.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci ASAL382245:GJJN-2729-MONOMER.

Family and domain databases

Gene3Di 2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPi MF_01417. SpeA.
InterProi IPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
IPR029066. PLP-binding_barrel.
[Graphical view ]
Pfami PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view ]
PIRSFi PIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSi PR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMi SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR01273. speA. 1 hit.
PROSITEi PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
    Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
    BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A449.

Entry informationi

Entry nameiSPEA_AERS4
AccessioniPrimary (citable) accession number: A4SPD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: November 26, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3