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P72587

- SPEA2_SYNY3

UniProt

P72587 - SPEA2_SYNY3

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Protein

Biosynthetic arginine decarboxylase 2

Gene

speA2

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.By similarity

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Magnesium.By similarity
Pyridoxal phosphate.By similarity

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

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylase 2 (EC:4.1.1.19)
Short name:
ADC 2
Gene namesi
Name:speA2
Synonyms:speA
Ordered Locus Names:slr1312
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659Biosynthetic arginine decarboxylase 2PRO_0000149982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei119 – 1191N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP72587.

Interactioni

Protein-protein interaction databases

STRINGi1148.slr1312.

Structurei

3D structure databases

ProteinModelPortaliP72587.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 32111Substrate-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiP72587.
KOiK01585.
OMAiCCVESAV.
OrthoDBiEOG676Z0R.
PhylomeDBiP72587.

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.
IPR022653. De-COase2_pyr-phos_BS.
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.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P72587 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGEEPVPADK ALGKKFKKKN ASWSIEESEA LYRVEAWGAP YFAINAAGNI
60 70 80 90 100
TVSPNGDRGG SLDLLELVEA LRQRKLGLPL LIRFSDILAD RLERLNSCFA
110 120 130 140 150
KAIARYNYPN TYQAVYPVKC NQQRHLVEAL VRFGQTSQCG LEAGSKPELM
160 170 180 190 200
IALATLPPPL DRQDKHTKPL IICNGYKDQD YLETALLAKR LGHRPIIIIE
210 220 230 240 250
QLRELEWVLH ISQQLNIKPM LGVRARLSCQ SLKSSEISSG NGDRAKLGLT
260 270 280 290 300
MPDIVTVIHR LEENNCLDCL KMLHFHLGTQ VSDIALIKEA MREASQLYVE
310 320 330 340 350
LVKLGAKMRY LNVGGGLAVD YDGSKTNYPA SKNYNMQNYA NDIVAAIQDA
360 370 380 390 400
CELGQVSPPI LVSESGRAIM AHQSVLVFDV LGSNQTGFSE PHPPDENAHP
410 420 430 440 450
LLKNLWECYE TITAEQYQEQ YHDALQLKTE ASSLFNFGYL SLTERGQAEQ
460 470 480 490 500
IHWACCRKIF EITRQLEYIP EDFQALDKIM TDIYYVNLSV FQSAPESWSL
510 520 530 540 550
DQLFPILPIH HLNEKPSQRV ILADLTCDSD GKIDRFIDLW DVKSYLEVHP
560 570 580 590 600
LENDGNPYYL GMFLVGAYQE IMGNLHNLFG DINVVHIATT PQGYQIESVV
610 620 630 640 650
RGDTMTEVLG YVQYDSDDLL EGLRRHTELA LSNGQITLEE SRRLLEDYEQ

SLRRYTYLS
Length:659
Mass (Da):74,477
Last modified:February 1, 1997 - v1
Checksum:iE8442002C8CD4629
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000022 Genomic DNA. Translation: BAA16587.1.
X96602 Genomic DNA. Translation: CAA65422.1.
PIRiS74435.
RefSeqiNP_439907.1. NC_000911.1.
YP_005649962.1. NC_017277.1.
YP_007449790.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA16587; BAA16587; BAA16587.
GeneIDi951929.
KEGGisyn:slr1312.
syy:SYNGTS_0009.
syz:MYO_190.
PATRICi23836874. VBISynSp132158_0012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000022 Genomic DNA. Translation: BAA16587.1 .
X96602 Genomic DNA. Translation: CAA65422.1 .
PIRi S74435.
RefSeqi NP_439907.1. NC_000911.1.
YP_005649962.1. NC_017277.1.
YP_007449790.1. NC_020286.1.

3D structure databases

ProteinModelPortali P72587.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 1148.slr1312.

Proteomic databases

PRIDEi P72587.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA16587 ; BAA16587 ; BAA16587 .
GeneIDi 951929.
KEGGi syn:slr1312.
syy:SYNGTS_0009.
syz:MYO_190.
PATRICi 23836874. VBISynSp132158_0012.

Phylogenomic databases

eggNOGi COG1166.
HOGENOMi HOG000029191.
InParanoidi P72587.
KOi K01585.
OMAi CCVESAV.
OrthoDBi EOG676Z0R.
PhylomeDBi P72587.

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.
IPR022653. De-COase2_pyr-phos_BS.
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 SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR01273. speA. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.
  2. "Disruption of a spe-like open reading frame alters polyamine content and psbA-2 mRNA stability in the cyanobacterium Synechocystis sp. PCC 6803."
    Mulo P., Eloranta T., Aro E.M., Maenpaeae P.
    Bot. Acta 111:71-76(1998)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-302.

Entry informationi

Entry nameiSPEA2_SYNY3
AccessioniPrimary (citable) accession number: P72587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 102 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

External Data

Dasty 3