Skip Header

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

Q87F25

- SPEA_XYLFT

UniProt

Q87F25 - SPEA_XYLFT

(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
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Status
Reviewed - Annotation score: 2 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

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

BioCyciXFAS183190:GIX4-113-MONOMER.

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:PD_0113
OrganismiXylella fastidiosa (strain Temecula1 / ATCC 700964)
Taxonomic identifieri183190 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
ProteomesiUP000002516: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 628628Biosynthetic arginine decarboxylasePRO_0000149990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi183190.PD0113.

Structurei

3D structure databases

ProteinModelPortaliQ87F25.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni279 – 28911Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1166.
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.
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.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q87F25 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTWSQDLAHK TYSIRHWADG YFEVNDAGHM VVMPLGGDGV RISLPEVVDA
60 70 80 90 100
ARAAGAKLPL LLRFPDILGH RLGKLQAAFA QAQSEWEYAG GYTAVYPIKV
110 120 130 140 150
NQHRGVAGVL ASHQGDGFGL EAGSKPELMA VLALSRPGGL IVCNGYKDRE
160 170 180 190 200
YIRLALIGRK LGLKTFIVIE KPSELRMVLE EAKTLDVLPG LGVRVRLASL
210 220 230 240 250
GAGKWQNSGG DKAKFGLSPR QVLDVWKVLR GTEYADCLNV MHFHMGSQIS
260 270 280 290 300
NVRDIAKGMR EATRYFVELS RLGAKITHVD VGGGLGIDYE GTRSRSDCSI
310 320 330 340 350
NYGLQAYASH IVQPLASACE DYDLVPPRIV TECGRAMTAH HAVLIANVTE
360 370 380 390 400
VEAVPEGRVP GVCDDEPAVV RHMREIYGEL DARPAIELFY EAQHFHAEGL
410 420 430 440 450
AAYTLGQIDL VHRARIDDLF YAISHGVRER LSHEEKSHRP VLDELNERLV
460 470 480 490 500
DKYFVNFSVF ESIPDVWAIN QIFPIVPIER LNEVPTRRGV VCDLTCDSDG
510 520 530 540 550
TVKQYVENES LDSALPLHVL RHGEAYRIGF FLVGAYQEIL GDIHNLFGDT
560 570 580 590 600
DAVEVAVDGR GYRIAQQRCG DTTDVMLDYV GYALDEVRRV YAQRIAAAGM
610 620
SAAESKALSD MLEAGLTGYP YLSDVPLE
Length:628
Mass (Da):69,214
Last modified:June 1, 2003 - v1
Checksum:i0E820F250B06A04A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009442 Genomic DNA. Translation: AAO28012.1.
RefSeqiNP_778363.1. NC_004556.1.

Genome annotation databases

EnsemblBacteriaiAAO28012; AAO28012; PD_0113.
GeneIDi1144325.
KEGGixft:PD0113.
PATRICi24147641. VBIXylFas71109_0156.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009442 Genomic DNA. Translation: AAO28012.1 .
RefSeqi NP_778363.1. NC_004556.1.

3D structure databases

ProteinModelPortali Q87F25.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 183190.PD0113.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO28012 ; AAO28012 ; PD_0113 .
GeneIDi 1144325.
KEGGi xft:PD0113.
PATRICi 24147641. VBIXylFas71109_0156.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci XFAS183190:GIX4-113-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.
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 PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa."
    Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M.
    , Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.
    J. Bacteriol. 185:1018-1026(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Temecula1 / ATCC 700964.

Entry informationi

Entry nameiSPEA_XYLFT
AccessioniPrimary (citable) accession number: Q87F25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2003
Last modified: October 1, 2014
This is version 72 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3