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A3QDD8

- SPEA_SHELP

UniProt

A3QDD8 - SPEA_SHELP

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
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

BioCyciSLOI323850:GHQJ-1675-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:Shew_1619
OrganismiShewanella loihica (strain ATCC BAA-1088 / PV-4)
Taxonomic identifieri323850 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001558: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_1000024269Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi323850.Shew_1619.

Structurei

3D structure databases

ProteinModelPortaliA3QDD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 29611Substrate-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.
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.

A3QDD8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNWSIKDAY VGYNVNYWSS GLYGISEAGE VTVSPDPNHP EHTIGLNELA
60 70 80 90 100
KDMVKSGVAL PVLVRFPQIL HHRVNSLCNA FNQAITRYDY QSDYLLVYPI
110 120 130 140 150
KVNQQQTVVE EILASQVSKE VPQLGLEAGS KPELMAVLAM AQKASSVIIC
160 170 180 190 200
NGYKDVEYIR LALIGEKLGH QVYIVLEKLS ELKVVLEEAK KLGVTPRLGL
210 220 230 240 250
RVRLAFQGKG KWQASGGEKS KFGLSAAQVL NVINSLKDED MLDSLQLLHF
260 270 280 290 300
HLGSQIANIR DIRSGVSEAG RFYCELQKMG ANVKCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSSNSMNYG LTEYANNIVS VLNDMCREHD QPMPRLISES GRYLTAHHAV
360 370 380 390 400
LITDVIGTEA YKPEDLQAPD EEAPQQLKNM WDSWGEVSGR ADQRALIEIY
410 420 430 440 450
HDVQSDLAEV HSLFALGQMS LSDRAWAEQM NLRVCYELKG VMSGKYRFHR
460 470 480 490 500
PVIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPVMPLS GLDKKPERRA
510 520 530 540 550
VMLDITCDSD GTVDQYVDGQ GIETTLPVPA WSAESPYLIG FFLVGAYQEI
560 570 580 590 600
LGDMHNLFGD TNSAVVRLDD DGLVNIESVL AGDTVADVLR YVNLDAVSFM
610 620 630
RTYEELVNLH IQEDERANIL EELQIGLKGY TYLEDFS
Length:637
Mass (Da):71,014
Last modified:April 17, 2007 - v1
Checksum:i3A1D81837D2B9896
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000606 Genomic DNA. Translation: ABO23486.1.
RefSeqiYP_001093745.1. NC_009092.1.

Genome annotation databases

EnsemblBacteriaiABO23486; ABO23486; Shew_1619.
GeneIDi4922250.
KEGGislo:Shew_1619.
PATRICi23515073. VBISheLoi132094_1623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000606 Genomic DNA. Translation: ABO23486.1 .
RefSeqi YP_001093745.1. NC_009092.1.

3D structure databases

ProteinModelPortali A3QDD8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 323850.Shew_1619.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO23486 ; ABO23486 ; Shew_1619 .
GeneIDi 4922250.
KEGGi slo:Shew_1619.
PATRICi 23515073. VBISheLoi132094_1623.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SLOI323850:GHQJ-1675-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.
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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1088 / PV-4.

Entry informationi

Entry nameiSPEA_SHELP
AccessioniPrimary (citable) accession number: A3QDD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: November 26, 2014
This is version 54 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