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A6WM65

- SPEA_SHEB8

UniProt

A6WM65 - SPEA_SHEB8

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella baltica (strain OS185)
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

BioCyciSBAL402882:GJ99-1808-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:Shew185_1761
OrganismiShewanella baltica (strain OS185)
Taxonomic identifieri402882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000006387: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_1000024266Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi402882.Shew185_1761.

Structurei

3D structure databases

ProteinModelPortaliA6WM65.
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.

A6WM65-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNDWSIDDAR AGYNVTHWSQ GFYGISDHGE VTVSPDPKNP DYKIGLNELA
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 LVVEQLKQND MLDSLQLLHF
260 270 280 290 300
HLGSQIANIR DIRQGVSEAG RFYCELRALG ASVNCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSNNSMNYG LTEYANNIVN VLTDICNEYE QPMPRIISES GRYLTAHHAV
360 370 380 390 400
LITDVIGTEA YQPEDIQPPA EESPQLLHNM WHSWSELSGR ADQRALIEIY
410 420 430 440 450
HDSQSDLQEA HSLFALGQLS LAERAWAEQA NLRVCHEVQG LLSAKNRYHR
460 470 480 490 500
PIIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPVLPLS GLDKAPERRA
510 520 530 540 550
VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSADSPYLIG FFLVGAYQEI
560 570 580 590 600
LGDMHNLFGD TNSAVVRIED NGVTNIESVL AGDTVADVLR YVNLDAVAFM
610 620 630
RTYEELVNLH IAEDERAQIL EELQVGLKGY TYLEDFS
Length:637
Mass (Da):70,894
Last modified:August 21, 2007 - v1
Checksum:iADF1EB11628530BF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000753 Genomic DNA. Translation: ABS07904.1.
RefSeqiYP_001365967.1. NC_009665.1.

Genome annotation databases

EnsemblBacteriaiABS07904; ABS07904; Shew185_1761.
GeneIDi5371239.
KEGGisbm:Shew185_1761.
PATRICi23460244. VBISheBal127872_1942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000753 Genomic DNA. Translation: ABS07904.1 .
RefSeqi YP_001365967.1. NC_009665.1.

3D structure databases

ProteinModelPortali A6WM65.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 402882.Shew185_1761.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS07904 ; ABS07904 ; Shew185_1761 .
GeneIDi 5371239.
KEGGi sbm:Shew185_1761.
PATRICi 23460244. VBISheBal127872_1942.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SBAL402882:GJ99-1808-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: OS185.

Entry informationi

Entry nameiSPEA_SHEB8
AccessioniPrimary (citable) accession number: A6WM65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: October 1, 2014
This is version 50 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