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Q0HW78

- SPEA_SHESR

UniProt

Q0HW78 - SPEA_SHESR

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Protein

Biosynthetic arginine decarboxylase

Gene
speA, Shewmr7_1632
Organism
Shewanella sp. (strain MR-7)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine By similarity.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation
Pyridoxal phosphate By similarity.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

BioCyciSSP60481:GHW6-1716-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Gene namesi
Name:speA
Ordered Locus Names:Shewmr7_1632
OrganismiShewanella sp. (strain MR-7)
Taxonomic identifieri60481 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001960: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylaseUniRule annotationPRO_1000024273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Protein-protein interaction databases

STRINGi60481.Shewmr7_1632.

Structurei

3D structure databases

ProteinModelPortaliQ0HW78.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 29611Substrate-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

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.

Q0HW78-1 [UniParc]FASTAAdd to Basket

« Hide

MNDWSIDAAR AGYNVTHWSQ GFYGISDQGE VTVSPDPKNP DHKIGLNELA    50
KDMVKAGVAL PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI 100
KVNQQKTVVE EILASQASKE VPQLGLEAGS KPELMAVLAM AQKASSVIVC 150
NGYKDNEYIR LALIGEKLGH KVYIVLEKLS ELKMVLAESK RLGVKPRLGL 200
RARLAFQGKG KWQASGGEKS KFGLSAAQIL TVVDQLKEND MLDSLQLLHF 250
HLGSQIANIR DIRQGVSEAA RFYCELRELG ASINCFDVGG GLAVDYDGTR 300
SQSNNSMNYG LSEYANNIVN VLTDICNEYE QPMPRIISES GRHLTAHHAV 350
LITDVIGTEA YQVEDIQPPA EESPQLLHNM WQSWTELSGR ADQRALIEIY 400
HDSQSDLQEA QSLFALGQLS LAERAWAEQA NLRVCHEVQG LLSTKNRYHR 450
PIIDELNEKL ADKFFVNFSL FQSLPDAWGI DQVFPVLPLS GLDKAPERRA 500
VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSAESPYLMG FFMVGAYQEI 550
LGDMHNLFGD TNSAVVSIEE NGMTNIESVL AGDTVADVLR YVNLDAVDFM 600
RTYEELVNQH IVEEERAQIL EELQVGLKGY TYLEDFS 637
Length:637
Mass (Da):71,019
Last modified:October 3, 2006 - v1
Checksum:i1E26995E7BB168BD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000444 Genomic DNA. Translation: ABI42627.1.
RefSeqiYP_737684.1. NC_008322.1.

Genome annotation databases

EnsemblBacteriaiABI42627; ABI42627; Shewmr7_1632.
GeneIDi4257085.
KEGGishm:Shewmr7_1632.
PATRICi23588327. VBISheSp85603_1687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000444 Genomic DNA. Translation: ABI42627.1 .
RefSeqi YP_737684.1. NC_008322.1.

3D structure databases

ProteinModelPortali Q0HW78.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 60481.Shewmr7_1632.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI42627 ; ABI42627 ; Shewmr7_1632 .
GeneIDi 4257085.
KEGGi shm:Shewmr7_1632.
PATRICi 23588327. VBISheSp85603_1687.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci SSP60481:GHW6-1716-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: MR-7.

Entry informationi

Entry nameiSPEA_SHESR
AccessioniPrimary (citable) accession number: Q0HW78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: June 11, 2014
This is version 58 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

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