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A1AS90

- SPEA_PELPD

UniProt

A1AS90 - SPEA_PELPD

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Pelobacter propionicus (strain DSM 2379)
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

Magnesium.UniRule annotation
Pyridoxal phosphate.UniRule 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

BioCyciPPRO338966:GHL0-2647-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:Ppro_2606
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000006732: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 635635Biosynthetic arginine decarboxylasePRO_1000068492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi338966.Ppro_2606.

Structurei

3D structure databases

ProteinModelPortaliA1AS90.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 29211Substrate-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.
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.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1AS90 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERWSINDSA KIYNLNNWGG DLFSINKKGN ICVHPSPNSK YSIELASLVD
60 70 80 90 100
DLIKRKIKPP ILLRFMNILE GRIASINRVF RNAIQTNNYP AQYQTFYPIK
110 120 130 140 150
VNQQRQVVEA IANFGKKYNI GLEVGSKPEL VAAISISTNN SLPIICNGYK
160 170 180 190 200
DTEFIETVLY ATKIGYNITI VIEKLFELEK VIELSRKTGI TPKLGIRVKL
210 220 230 240 250
SSKGTGKWAT SGGEDAKFGL RISEIITAID LLKQYNLIDS VKLLHSHIGS
260 270 280 290 300
QVTKIDKIKN ALIEGARIYV EMKKLGVNLE YIDIGGGLGV DYDGSKSSYF
310 320 330 340 350
SSVNYSVEEY ANDVIYQIKN ICDEAGVDCP NIISESGRAT VAHYSVMVTN
360 370 380 390 400
ILNTNTQNQM PDFESILTQA EPLSPTVRKL VDIYKSIDRH SLREDYHDTL
410 420 430 440 450
QLIQEAVSLF NLGYLNLNDR AMAEWLYTRI IKKINNLVEK MKPVPEELQN
460 470 480 490 500
FKLSMRQTYF ANFSLFQSIP DSWAIDQLFP IMPIQRLGEK PDVIASIADI
510 520 530 540 550
TCDSDGEITS FVGENGRTKY LPLHKIRKNE EYYIGFFLIG AYQEILGDLH
560 570 580 590 600
NLFGDTNAVH ITFNKKTNYR IDTVISGDAI QQSLKYVQYD GNEILKKVRD
610 620 630
SLENGVASKK ISIEESSHFL ELLDKTIQAY TYLGE
Length:635
Mass (Da):71,801
Last modified:January 23, 2007 - v1
Checksum:iA1A77BF7734E5614
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000482 Genomic DNA. Translation: ABL00211.1.
RefSeqiWP_011736464.1. NC_008609.1.
YP_902268.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABL00211; ABL00211; Ppro_2606.
GeneIDi4572939.
KEGGippd:Ppro_2606.
PATRICi22898311. VBIPelPro64470_2761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000482 Genomic DNA. Translation: ABL00211.1 .
RefSeqi WP_011736464.1. NC_008609.1.
YP_902268.1. NC_008609.1.

3D structure databases

ProteinModelPortali A1AS90.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 338966.Ppro_2606.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL00211 ; ABL00211 ; Ppro_2606 .
GeneIDi 4572939.
KEGGi ppd:Ppro_2606.
PATRICi 22898311. VBIPelPro64470_2761.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci PPRO338966:GHL0-2647-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.
IPR022653. De-COase2_pyr-phos_BS.
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 SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR01273. speA. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiSPEA_PELPD
AccessioniPrimary (citable) accession number: A1AS90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 53 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, Reference proteome

Documents

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

External Data

Dasty 3