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B0TQX3

- SPEA_SHEHH

UniProt

B0TQX3 - SPEA_SHEHH

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Shewanella halifaxensis (strain HAW-EB4)
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

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: 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 8, 2008 - v1
Checksum:i17A13A3F53418DA9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000931 Genomic DNA. Translation: ABZ76368.1.
RefSeqiWP_012276901.1. NC_010334.1.
YP_001674027.1. NC_010334.1.

Genome annotation databases

EnsemblBacteriaiABZ76368; ABZ76368; Shal_1803.
GeneIDi5902856.
KEGGishl:Shal_1803.
PATRICi23506281. VBISheHal24697_1891.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000931 Genomic DNA. Translation: ABZ76368.1 .
RefSeqi WP_012276901.1. NC_010334.1.
YP_001674027.1. NC_010334.1.

3D structure databases

ProteinModelPortali B0TQX3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 458817.Shal_1803.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABZ76368 ; ABZ76368 ; Shal_1803 .
GeneIDi 5902856.
KEGGi shl:Shal_1803.
PATRICi 23506281. VBISheHal24697_1891.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SHAL458817:GH1X-1862-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: HAW-EB4.

Entry informationi

Entry nameiSPEA_SHEHH
AccessioniPrimary (citable) accession number: B0TQX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: October 29, 2014
This is version 48 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