Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q46I12 (Q46I12_PROMT) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase HAMAP MF_01417
Short name=ADC HAMAP MF_01417
EC=4.1.1.19 HAMAP MF_01417
Gene names
Name:speA HAMAP MF_01417
Ordered Locus Names:PMN2A_1378
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP] EMBL AAZ58866.1
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP MF_01417 SAAS SAAS009006

Catalytic activity

L-arginine = agmatine + CO2. HAMAP MF_01417 RuleBase RU003740 SAAS SAAS009006

Cofactor

Magnesium By similarity. HAMAP MF_01417 RuleBase RU003740 SAAS SAAS009006

Pyridoxal phosphate By similarity. HAMAP MF_01417 SAAS SAAS000183

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP MF_01417

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. HAMAP MF_01417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region290 – 30011Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue1081N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
Q46I12 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: FF5A6848F9E8C041

FASTA64772,462
        10         20         30         40         50         60 
MAVKITNQSL SWTIQNSSEL YGIDRWGKGY FTINEKGNIS ICPNGSNNKS HDLMELLDEL 

        70         80         90        100        110        120 
ESRKLKFPLL IRFDDILEDC LKNLHKAFEK AINDYQYQGK YQGVFPIKCN QQRHVVEELI 

       130        140        150        160        170        180 
TCGSKWNFGL EAGSKPELLI ALSILEDPKA LLICNGYKDQ RYIETAILAR QLGRQPIVVI 

       190        200        210        220        230        240 
EQANDVELII KSSNLLGASP LIGIRAKLSS QSSGRWSSSI GDKSKFGLSI PEILKAIKRL 

       250        260        270        280        290        300 
KEANLLNELK LLHFHLGSQI NDIGVLKDAL QEAGQIYAEL INLGAPMGYL DVGGGLGIDY 

       310        320        330        340        350        360 
DGSQTASIAS TNYSLQNYAN DVVATIKECC ESKKIPLPTL ITESGRAIAS HFSILIFNIL 

       370        380        390        400        410        420 
GKNSLPSDIP KENEKECLSV RNLRETLVHI NSLELKQEKD LAKLQEAWND SLKFKADALA 

       430        440        450        460        470        480 
AFRLGYIDLV ERAKAEQLTW ACAKTIVNQL PKNILLPKEL KKLSESLAVT YYANLSVFRS 

       490        500        510        520        530        540 
APDTWAIDQV FPIMPIHRLS KEPKKLGHFA DLTCDSDGKL DQFIDNGKIK NLLPLHEFNQ 

       550        560        570        580        590        600 
NEKYLIGLFL GGAYQEVMGN LHNLFGSTNA VHIRFTENGN YKVEHVIRGN TKSNVLEYLE 

       610        620        630        640 
HDPEILLERL RKSSELAIQG GHLKIHDAQK LIEHVEASLR QSTYLQS

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000095 Genomic DNA. Translation: AAZ58866.1.
RefSeqYP_292569.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46I12.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ46I12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3606773.
GenomeReviewsGene locus PMN2A_1378 in contig CP000095_GR.
KEGGpmn:PMN2A_1378.
PATRIC23022181. VBIProMar14922_0051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBQ46I12.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycPMAR59920:PMN2A_1378-MONOMER.

Family and domain databases

HAMAPMF_01417. SpeA.
[Tree]
InterProIPR009006. 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.
[Graphical view]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits.
KOK01585.
PANTHERPTHR11482:SF3. Arg_decrbxlase. 1 hit.
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
TIGRFAMsTIGR01273. SpeA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ46I12_PROMT
AccessionPrimary (citable) accession number: Q46I12
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info