Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q31DD8

- SPEA_PROM9

UniProt

Q31DD8 - SPEA_PROM9

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Prochlorococcus marinus (strain MIT 9312)
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

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

BioCyciPMAR74546:GHRG-46-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:PMT9312_0046
OrganismiProchlorococcus marinus (strain MIT 9312)
Taxonomic identifieri74546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002715: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648Biosynthetic arginine decarboxylasePRO_1000024261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi74546.PMT9312_0046.

Structurei

3D structure databases

ProteinModelPortaliQ31DD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 30111Substrate-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.
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.

Q31DD8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNFEPKKLK NIWTIEDSIS TYNIDKWGDK YFSINSKGNI SVTKDIKSEN
60 70 80 90 100
KIDLFKLVKE LKSREINPPL IIRFNDILKD RINALHDSFF KAIKTYKYKN
110 120 130 140 150
IYQGVFPVKC NQQKNVLEKI IEFGSQWNFG LEVGSKSELL IGLALLENQN
160 170 180 190 200
SLLICNGYKD KKYIEIATLA RKLGKNPIIV IEQRDEVKRI IQAVQELNAT
210 220 230 240 250
PLIGIRAKLS SKSSGRWGKS IGDNSKFGLS IPEIMLTIKE LKEANLINEM
260 270 280 290 300
KLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LCKLGAPMQY IDVGGGLGID
310 320 330 340 350
FDGTKTSSNT STNYSLQNYA NDVIATIKDS CELNNIKHPI IISESGRAII
360 370 380 390 400
SHCSVLIFNV LGTSHVSSKL QIFDKKNQQL IISNLLETFY ELKKLKNKKI
410 420 430 440 450
NLSQIIELWN DAKKFKEDCL VAFRLGFLSL AERAYAEELT WACAKEISKN
460 470 480 490 500
LNNDAINHPD LSEITETLAS TYYANLSIFK SIPDSWAINQ IFPIVPIHRH
510 520 530 540 550
LEEPFCKGNF ADLTCDSDGK LNNFIDDGKI KSLLNLHKPE EDKDYLIGIF
560 570 580 590 600
MTGAYQEALG NLHNLFGSTN VVHIDINQDN SYKVKNIIKE DSKSEILQLL
610 620 630 640
DYSSASLVES IRINTESAID QKKLTIEEAR KLMDQIEISL RKSSYLSE
Length:648
Mass (Da):73,366
Last modified:December 6, 2005 - v1
Checksum:i7F89743E16C3B08A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000111 Genomic DNA. Translation: ABB49107.1.
RefSeqiWP_011375611.1. NC_007577.1.
YP_396543.1. NC_007577.1.

Genome annotation databases

EnsemblBacteriaiABB49107; ABB49107; PMT9312_0046.
GeneIDi3764827.
KEGGipmi:PMT9312_0046.
PATRICi23003698. VBIProMar70153_0046.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000111 Genomic DNA. Translation: ABB49107.1 .
RefSeqi WP_011375611.1. NC_007577.1.
YP_396543.1. NC_007577.1.

3D structure databases

ProteinModelPortali Q31DD8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74546.PMT9312_0046.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB49107 ; ABB49107 ; PMT9312_0046 .
GeneIDi 3764827.
KEGGi pmi:PMT9312_0046.
PATRICi 23003698. VBIProMar70153_0046.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci PMAR74546:GHRG-46-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. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9312.

Entry informationi

Entry nameiSPEA_PROM9
AccessioniPrimary (citable) accession number: Q31DD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: November 26, 2014
This is version 60 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