SubmitCancel

Skip Header

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

Q7TUJ9

- SPEA_PROMM

UniProt

Q7TUJ9 - SPEA_PROMM

(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, PMT_2150
Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed - Annotation score: 2 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

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 (EC:4.1.1.19)
Short name:
ADC
Gene namesi
Name:speA
Ordered Locus Names:PMT_2150
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001423: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648Biosynthetic arginine decarboxylaseUniRule annotationPRO_0000149969Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi74547.PMT2150.

Structurei

3D structure databases

ProteinModelPortaliQ7TUJ9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 30111Substrate-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

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.
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.

Q7TUJ9-1 [UniParc]FASTAAdd to Basket

« Hide

MSAADPIQDN KSWTVADSAA LYGLDHWGHP YFSANANGHV QVQPRGDQGS    50
CLDLVELVEE LKSRNLNLPL LIRFDDILED RLERLHSAFE EAISKYGYAG 100
RYQGVFPVKC NQQRHVVEQL VESGRQWHFG LEAGSKAELL IALSLVNDPE 150
ALLICNGYKD QRYIETAILA RRLGRQPVVV IEQPDEVERI IRSSQELGAA 200
PFLGVRAKLT TRSTGHWSSS VGEKAKFGLS VPDLLATVEA LRQADLLSDL 250
RLLHFHIGSQ INDIAVLKDA LQEAAQIYVE LTKLGAPMGY LDVGGGLGVD 300
YDGSRSASAA STNYSLQNYA NDVVATVREC CKPHGITLPI LVSESGRAIA 350
SHFSILVFDV LGTGTVPGAI PKQTVEEPLT IHNLRETLSG VMATQKGAVS 400
EISRLQEAWN DAIKFKEDAL AAFRLGYISL PERALAEQLT GACAEAIMGQ 450
LPCNETIPDD LQSLRAVLAS TYYANLSIFR SAPDTWAIEQ LFPLMPIHRL 500
NEEPTQLGHF ADLTCDSDGK LDRFIGNGQT KTLLELHNLR QNEAYMIGMF 550
LAGAYQEVMG NLHNLFGSTN AVHIRLTTAG GYQVDHVVRG NTNSEVLEAM 600
EHNPELLLER LRLASELAIQ RGELKINDVR RLMDHLEASL RQTTYLQG 648
Length:648
Mass (Da):71,364
Last modified:October 1, 2003 - v1
Checksum:iBBFEE45E4F8E395B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE22324.1.
RefSeqiNP_895974.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE22324; CAE22324; PMT_2150.
GeneIDi1727896.
KEGGipmt:PMT2150.
PATRICi23013213. VBIProMar135351_2729.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE22324.1 .
RefSeqi NP_895974.1. NC_005071.1.

3D structure databases

ProteinModelPortali Q7TUJ9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74547.PMT2150.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE22324 ; CAE22324 ; PMT_2150 .
GeneIDi 1727896.
KEGGi pmt:PMT2150.
PATRICi 23013213. VBIProMar135351_2729.

Phylogenomic databases

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

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: MIT 9313.

Entry informationi

Entry nameiSPEA_PROMM
AccessioniPrimary (citable) accession number: Q7TUJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 67 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

Similar proteinsi