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A2BNH3

- SPEA_PROMS

UniProt

A2BNH3 - SPEA_PROMS

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Protein

Biosynthetic arginine decarboxylase

Gene
speA, A9601_00461
Organism
Prochlorococcus marinus (strain AS9601)
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

BioCyciPMAR146891:GH90-47-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:A9601_00461
OrganismiProchlorococcus marinus (strain AS9601)
Taxonomic identifieri146891 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002590: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648Biosynthetic arginine decarboxylaseUniRule annotationPRO_1000024262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Protein-protein interaction databases

STRINGi146891.A9601_00461.

Structurei

3D structure databases

ProteinModelPortaliA2BNH3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 30111Substrate-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.
IPR022657. De-COase2_CS.
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.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2BNH3-1 [UniParc]FASTAAdd to Basket

« Hide

MTNFEPKKFK NIWTIEDSIS SYNIDKWGDK YFSINSKGNI SVTKDIKSEN    50
KIDLFKLVKE LKSREINPPL IIRFNDILKD RINALHDSFL KAIKTYKYKN 100
IYQGVFPVKC NQQKNVLEKI IEFGSQWNFG LEVGSKSELL IGLALLENQN 150
SLLICNGYKD KKYIEIATLA RKLGKNPIIV IEQRDEVKRI IQAVQELKAT 200
PLIGIRAKLS SKSSGRWGKS IGDNSKFGLS IPEIMLTIKE LKEANLINEM 250
KLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LCKLGAPMQY IDVGGGLGID 300
FDGTKTSSNT STNYSLQNYA NDVIATIKDS CELNNIKHPT IISESGRAII 350
SHCSVLIFNV LGTSHVSSKL QIFDKKNQQL IISNLLDTFY ELKKLKNKKI 400
NLSQIIELWN DAKKFKEDCL VAFRLGFLSL AERAYAEELT WACAKEISNN 450
LNNDEINHPD LSEITETLAS TYYANLSIFK SIPDSWAINQ IFPIVPIHRH 500
LEEPFCKGNF ADLTCDSDGK LNNFIDNGKI KSLLNLHKPE EDKDYLIGIF 550
MTGAYQEALG NLHNLFGSTN VVHIDINQDN SYKVRNIIKE DSKSEILQLL 600
DYSSASLVES IRINTESAID QKKLTIEEAR KLMDQIEISL RKSSYLSE 648
Length:648
Mass (Da):73,411
Last modified:February 20, 2007 - v1
Checksum:iEEB5C31FA2471039
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000551 Genomic DNA. Translation: ABM69334.1.
RefSeqiWP_011817524.1. NC_008816.1.
YP_001008441.1. NC_008816.1.

Genome annotation databases

EnsemblBacteriaiABM69334; ABM69334; A9601_00461.
GeneIDi4716728.
KEGGipmb:A9601_00461.
PATRICi22981537. VBIProMar75723_0047.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000551 Genomic DNA. Translation: ABM69334.1 .
RefSeqi WP_011817524.1. NC_008816.1.
YP_001008441.1. NC_008816.1.

3D structure databases

ProteinModelPortali A2BNH3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 146891.A9601_00461.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM69334 ; ABM69334 ; A9601_00461 .
GeneIDi 4716728.
KEGGi pmb:A9601_00461.
PATRICi 22981537. VBIProMar75723_0047.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci PMAR146891:GH90-47-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.
IPR022657. De-COase2_CS.
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.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AS9601.

Entry informationi

Entry nameiSPEA_PROMS
AccessioniPrimary (citable) accession number: A2BNH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: September 3, 2014
This is version 56 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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