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B0CB40 (B0CB40_ACAM1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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 EMBL ABW26679.1
Ordered Locus Names:AM1_1658
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Acaryochloris

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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

Region326 – 33611Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue1441N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
B0CB40 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 8256E0C859F0065C

FASTA67475,386
        10         20         30         40         50         60 
MENGRNREDR ATKISQTLAA ELENGHSAPM RERPLTSDPN PEQTDAAWSI EESEKLYRIR 

        70         80         90        100        110        120 
GWGEPYFSVN AAGHVTVSPK ADRGGSLDLY ELVQSLQQRD IHAPLLIRFS DILADRIERL 

       130        140        150        160        170        180 
NACFAKAIAR YSYPGRYRGV FPVKCNQQRH LVEDLVRFGQ PHQFGLEAGS KPELLIAIAS 

       190        200        210        220        230        240 
LKTSGALLIC NGYKDLEYVE TAMLAQRLGH QAIIVIEQLE EVELVIEASR RLQIQPILGV 

       250        260        270        280        290        300 
RAKLSAKGIG RWGTSAGDRA KFGLNIPEVV AAVEHLRAAN LLNSLQLLHF HIGSQISAIS 

       310        320        330        340        350        360 
VIKDALREAS QIYVELARLG ANMKFLDVGG GLGVDYDGSK SNSAASKNYN MQNYANDVVA 

       370        380        390        400        410        420 
EVKEACAEAD IPVPTLVSES GRAIASHQSV LIMNVLGSSD TLNLTPEPAQ ADEHLIIRNL 

       430        440        450        460        470        480 
WETYQTIDTE NYQEAYHDAL QFKEEAVSLF GFGYLSLEGR ARVERLCGAC CQRILAIARK 

       490        500        510        520        530        540 
DDDVAVDLED LERRMASLYY TNLSVFQSAP DTWAIDQLFP IMPIHRLEEE PTQRGTLVDL 

       550        560        570        580        590        600 
TCDSDGKIDQ FIYSRDTKPI LELHTLKPNE PYYLGMFLNG AYQEVMGNLH NLFGDTNVVH 

       610        620        630        640        650        660 
IDLTPMGYHI AHVVKGDTIT EVLEYVQYDA DDLIEEIRKQ SEVALQEQHI TLPEAQLLLK 

       670 
NYERSLRSYT YLKS

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References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000828 Genomic DNA. Translation: ABW26679.1.
RefSeqYP_001515993.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CB40.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0CB40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5680474.
GenomeReviewsGene locus AM1_1658 in contig CP000828_GR.
KEGGamr:AM1_1658.
PATRIC20617706. VBIAcaMar40141_1491.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBB0CB40.
ProtClustDBPRK05354.

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.
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR01273. SpeA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB0CB40_ACAM1
AccessionPrimary (citable) accession number: B0CB40
Entry history
Integrated into UniProtKB/TrEMBL: February 26, 2008
Last sequence update: February 26, 2008
Last modified: December 14, 2011
This is version 27 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