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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella halifaxensis (strain HAW-EB4)
Status
Reviewed-Annotation score: 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

BioCyciSHAL458817:GH1X-1862-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:Shal_1803
OrganismiShewanella halifaxensis (strain HAW-EB4)
Taxonomic identifieri458817 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001317 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_1000087407Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi458817.Shal_1803.

Structurei

3D structure databases

ProteinModelPortaliB0TQX3.
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.

B0TQX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNWSIDDAR ASYNVNHWSQ GLYGISDDGE VTVSPDPSRP ECKIGLNEMA
60 70 80 90 100
KDMVKSGVAL PVLVRFPQIL HHRVNSLCQA FNQAIQKYQY ENDYLLVYPI
110 120 130 140 150
KVNQQQTVVE EILASQVEKE VPQLGLEAGS KPELMAVLAM AQKASSVIIC
160 170 180 190 200
NGYKDKEYIR LALIGEKLGH KVYIVLEKIS ELKVVLEQAK ELGVTPRLGL
210 220 230 240 250
RVRLAFQGKG KWQASGGEKS KFGLSAAQVL QVITSLKQEN MLDSLELLHF
260 270 280 290 300
HLGSQIANIR DIRQGVSEAG RFYCELMKLG ANVKCFDVGG GLAVDYDGTR
310 320 330 340 350
SQSSHSMNYG LTEYANNIVS VLTDMCKEYE QPMPRIISES GRYLTAHHAV
360 370 380 390 400
LLTDVIGTEA YKPEDIQPPA EDAPQLLHNM WQSWVEVSGK ADQRALIEIF
410 420 430 440 450
HDCQSDLTEV HSLFAVGQVG LAERAWAEQV NLRVCYELQG SMSAKYRFHR
460 470 480 490 500
PIIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPVMPLS GLDKAPESRA
510 520 530 540 550
VMLDITCDSD GTIDQYVDGQ GIETTLPVPA WTQESPYLIG FFLVGAYQEI
560 570 580 590 600
LGDMHNLFGD TNSAVVRLDE DARTNVESVL AGDTVADVLR YVNLDAVSFM
610 620 630
RTYEELVNKH IAEDERANIL EELQLGLKGY TYLEDFS
Length:637
Mass (Da):71,120
Last modified:April 7, 2008 - v1
Checksum:i17A13A3F53418DA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000931 Genomic DNA. Translation: ABZ76368.1.
RefSeqiYP_001674027.1. NC_010334.1.

Genome annotation databases

EnsemblBacteriaiABZ76368; ABZ76368; Shal_1803.
KEGGishl:Shal_1803.
PATRICi23506281. VBISheHal24697_1891.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000931 Genomic DNA. Translation: ABZ76368.1.
RefSeqiYP_001674027.1. NC_010334.1.

3D structure databases

ProteinModelPortaliB0TQX3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi458817.Shal_1803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABZ76368; ABZ76368; Shal_1803.
KEGGishl:Shal_1803.
PATRICi23506281. VBISheHal24697_1891.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciSHAL458817:GH1X-1862-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HAW-EB4.

Entry informationi

Entry nameiSPEA_SHEHH
AccessioniPrimary (citable) accession number: B0TQX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 19, 2008
Last sequence update: April 7, 2008
Last modified: March 31, 2015
This is version 52 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.