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A1RKK8

- SPEA_SHESW

UniProt

A1RKK8 - SPEA_SHESW

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella sp. (strain W3-18-1)
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

BioCyciSSP351745:GCOY-2457-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:Sputw3181_2379
OrganismiShewanella sp. (strain W3-18-1)
Taxonomic identifieri351745 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002597: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_1000024274Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi351745.Sputw3181_2379.

Structurei

3D structure databases

ProteinModelPortaliA1RKK8.
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.

A1RKK8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNDWSIDDAR AGYNVTHWSQ GFYGISDQGE VTVSPDPKNP EYKIGLNELA
60 70 80 90 100
KDMVKAGVAL PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI
110 120 130 140 150
KVNQQQTVVE EILASQASKE VPQLGLEAGS KPELMAVLAM AQKASSVIVC
160 170 180 190 200
NGYKDNEYIR LALIGEKLGH KVYIVLEKLS ELKMVLAESK RLGVTPRLGL
210 220 230 240 250
RARLAFQGKG KWQASGGEKS KFGLSAAQIL TVVDQLKQND MLDSLQLLHF
260 270 280 290 300
HLGSQIANIR DIRQGVSEAG RFYCELRELG ASVNCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSNNSMNYG LTEYANNIVN VLTDICNEYA QPMPRIISES GRYLTAHHAV
360 370 380 390 400
LITDVIGTEA YQPENIQPPA EESPQLLHNM WHSWSEISGR ADQRALIEIY
410 420 430 440 450
HDSQSDLQEA QSLFALGQLS LAERAWAEQA NLRVCHEVQG LLSTKNRYHR
460 470 480 490 500
PIIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPVLPLS GLDKAPERRA
510 520 530 540 550
VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSAESPYLIG FFLVGAYQEI
560 570 580 590 600
LGDMHNLFGD TNSAVVRIEE NGVTNIESVL AGDTVADVLR YVNLDAVAFM
610 620 630
RTYEELVNLH IEEDERAQIL EELQVGLKGY TYLEDFS
Length:637
Mass (Da):70,979
Last modified:February 6, 2007 - v1
Checksum:i43F6C0DDFFF44E82
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000503 Genomic DNA. Translation: ABM25203.1.
RefSeqiYP_963757.1. NC_008750.1.

Genome annotation databases

EnsemblBacteriaiABM25203; ABM25203; Sputw3181_2379.
GeneIDi4660070.
KEGGishw:Sputw3181_2379.
PATRICi23598477. VBISheSp103602_2482.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000503 Genomic DNA. Translation: ABM25203.1 .
RefSeqi YP_963757.1. NC_008750.1.

3D structure databases

ProteinModelPortali A1RKK8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351745.Sputw3181_2379.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM25203 ; ABM25203 ; Sputw3181_2379 .
GeneIDi 4660070.
KEGGi shw:Sputw3181_2379.
PATRICi 23598477. VBISheSp103602_2482.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SSP351745:GCOY-2457-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: W3-18-1.

Entry informationi

Entry nameiSPEA_SHESW
AccessioniPrimary (citable) accession number: A1RKK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: October 1, 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