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B8EAI2

- SPEA_SHEB2

UniProt

B8EAI2 - SPEA_SHEB2

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella baltica (strain OS223)
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

BioCyciSBAL407976:GJ6Y-2607-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:Sbal223_2517
OrganismiShewanella baltica (strain OS223)
Taxonomic identifieri407976 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002507: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_1000184845Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi407976.Sbal223_2517.

Structurei

3D structure databases

ProteinModelPortaliB8EAI2.
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.

B8EAI2-1 [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:March 3, 2009 - v1
Checksum:iADF1EB11628530BF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001252 Genomic DNA. Translation: ACK47011.1.
RefSeqiYP_002358434.1. NC_011663.1.

Genome annotation databases

EnsemblBacteriaiACK47011; ACK47011; Sbal223_2517.
GeneIDi7087053.
KEGGisbp:Sbal223_2517.
PATRICi23481329. VBISheBal125792_2605.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001252 Genomic DNA. Translation: ACK47011.1 .
RefSeqi YP_002358434.1. NC_011663.1.

3D structure databases

ProteinModelPortali B8EAI2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 407976.Sbal223_2517.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACK47011 ; ACK47011 ; Sbal223_2517 .
GeneIDi 7087053.
KEGGi sbp:Sbal223_2517.
PATRICi 23481329. VBISheBal125792_2605.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SBAL407976:GJ6Y-2607-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: OS223.

Entry informationi

Entry nameiSPEA_SHEB2
AccessioniPrimary (citable) accession number: B8EAI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: October 1, 2014
This is version 38 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