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Q8PFQ5

- SPEA_XANAC

UniProt

Q8PFQ5 - SPEA_XANAC

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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Xanthomonas axonopodis pv. citri (strain 306)
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

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

BioCyciXAXO190486:GH55-3923-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:XAC3923
OrganismiXanthomonas axonopodis pv. citri (strain 306)
Taxonomic identifieri190486 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000000576: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 628628Biosynthetic arginine decarboxylasePRO_0000149987Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi190486.XAC3923.

Structurei

3D structure databases

ProteinModelPortaliQ8PFQ5.
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.
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.
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.

Q8PFQ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDWSLDQAR KTYSIPHWAD GYFDVNAAGH VVVTPTADGP AVSLPEVVDA
60 70 80 90 100
ARAAGAKLPL LVRFPDILGQ RLGKLQAAFA QAQSEWDYAG GYTAVYPIKV
110 120 130 140 150
NQHRGVAGTL ASHHGEGFGL EAGSKPELMA VLALSRPGGL IVCNGYKDRE
160 170 180 190 200
YIRLALIGRK LGLQTFIVIE KPSELTLVLE EARALDVKPG LGVRMRLASL
210 220 230 240 250
GAGKWQNSGG DKAKFGLSPR QVLDLWKTLR DTEYADSLNL LHFHMGSQIS
260 270 280 290 300
NVRDIANGMR EATRYFVELS RLGAKISHVD VGGGLGIDYE GTRSRSYCSI
310 320 330 340 350
NYGLHSYASN IVQPLASACE EHGLTPPRIV TECGRAMTAH HAVLIANVSE
360 370 380 390 400
VEQAPEGRVP DAHDDEPAAI RHLREIHDEL DVRPAVELFQ EAQHFHAEGL
410 420 430 440 450
SAYALGQIDL THRARIDDLF YAIAHGVRAR LSFDEKSHRP VLDELNERLV
460 470 480 490 500
DKYFVNFSVF ESIPDVWAID QVFPIVPIER LNEAPQRRGI IADMTCDSDG
510 520 530 540 550
MVKTYVENES LDSSLPLHRL NAGESYRIGF FLVGAYQEIL GDIHNLFGDT
560 570 580 590 600
DAVEVVVDRD GYRIAQQRRG DTTDVMLDYV GYQLDTLRAT YAERIAAAHL
610 620
SPERAQELSA ALEAGLTGYT YLSDEPLG
Length:628
Mass (Da):69,091
Last modified:March 29, 2004 - v2
Checksum:iCF03AC36E3066C05
GO

Sequence cautioni

The sequence AAM38760.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM38760.1. Different initiation.
RefSeqiNP_644224.2. NC_003919.1.

Genome annotation databases

EnsemblBacteriaiAAM38760; AAM38760; XAC3923.
GeneIDi1157994.
KEGGixac:XAC3923.
PATRICi24060012. VBIXanAxo33670_4051.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008923 Genomic DNA. Translation: AAM38760.1 . Different initiation.
RefSeqi NP_644224.2. NC_003919.1.

3D structure databases

ProteinModelPortali Q8PFQ5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 190486.XAC3923.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM38760 ; AAM38760 ; XAC3923 .
GeneIDi 1157994.
KEGGi xac:XAC3923.
PATRICi 24060012. VBIXanAxo33670_4051.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci XAXO190486:GH55-3923-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. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
    da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
    , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
    Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 306.

Entry informationi

Entry nameiSPEA_XANAC
AccessioniPrimary (citable) accession number: Q8PFQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: November 26, 2014
This is version 75 of the entry and version 2 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