P72587 (SPEA2_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biosynthetic arginine decarboxylase 2
Short name=ADC 2
EC=4.1.1.19

Gene names

Name:	speA2
Synonyms:	speA
Ordered Locus Names:	slr1312

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	659 AA.
Sequence status	Complete.
Protein existence	Inferred 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
Cofactor	Magnesium By similarity. HAMAP MF_01417 Pyridoxal phosphate By similarity. HAMAP MF_01417
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Spermidine biosynthesis
Ligand	Magnesium Metal-binding Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine catabolic process Inferred from electronic annotation. Source: InterPro spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	arginine decarboxylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 659	659	Biosynthetic arginine decarboxylase 2 HAMAP MF_01417		PRO_0000149982
Regions
	Region	311 – 321	11	Substrate-binding Potential
Amino acid modifications
	Modified residue	119	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P72587 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: E8442002C8CD4629	FASTA	659	74,477
	10 20 30 40 50 60 MGEEPVPADK ALGKKFKKKN ASWSIEESEA LYRVEAWGAP YFAINAAGNI TVSPNGDRGG 70 80 90 100 110 120 SLDLLELVEA LRQRKLGLPL LIRFSDILAD RLERLNSCFA KAIARYNYPN TYQAVYPVKC 130 140 150 160 170 180 NQQRHLVEAL VRFGQTSQCG LEAGSKPELM IALATLPPPL DRQDKHTKPL IICNGYKDQD 190 200 210 220 230 240 YLETALLAKR LGHRPIIIIE QLRELEWVLH ISQQLNIKPM LGVRARLSCQ SLKSSEISSG 250 260 270 280 290 300 NGDRAKLGLT MPDIVTVIHR LEENNCLDCL KMLHFHLGTQ VSDIALIKEA MREASQLYVE 310 320 330 340 350 360 LVKLGAKMRY LNVGGGLAVD YDGSKTNYPA SKNYNMQNYA NDIVAAIQDA CELGQVSPPI 370 380 390 400 410 420 LVSESGRAIM AHQSVLVFDV LGSNQTGFSE PHPPDENAHP LLKNLWECYE TITAEQYQEQ 430 440 450 460 470 480 YHDALQLKTE ASSLFNFGYL SLTERGQAEQ IHWACCRKIF EITRQLEYIP EDFQALDKIM 490 500 510 520 530 540 TDIYYVNLSV FQSAPESWSL DQLFPILPIH HLNEKPSQRV ILADLTCDSD GKIDRFIDLW 550 560 570 580 590 600 DVKSYLEVHP LENDGNPYYL GMFLVGAYQE IMGNLHNLFG DINVVHIATT PQGYQIESVV 610 620 630 640 650 RGDTMTEVLG YVQYDSDDLL EGLRRHTELA LSNGQITLEE SRRLLEDYEQ SLRRYTYLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.
[2]	"Disruption of a spe-like open reading frame alters polyamine content and psbA-2 mRNA stability in the cyanobacterium Synechocystis sp. PCC 6803." Mulo P., Eloranta T., Aro E.M., Maenpaeae P. Bot. Acta 111:71-76(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-302.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA16587.1. X96602 Genomic DNA. Translation: CAA65422.1.
PIR	S74435.
RefSeq	NP_439907.1. NC_000911.1.
3D structure databases
ProteinModelPortal	P72587.
ModBase	Search...
Protein-protein interaction databases
STRING	P72587.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	951929.
GenomeReviews	Gene locus slr1312 in contig BA000022_GR.
KEGG	syn:slr1312.
NMPDR	fig|1148.1.peg.8.
PATRIC	23836874. VBISynSp132158_0012.
Phylogenomic databases
eggNOG	COG1166.
HOGENOM	HBG321436.
OMA	FIANSSG.
PhylomeDB	P72587.
ProtClustDB	PRK05354.
Enzyme and pathway databases
BioCyc	SSP1148:SLR1312-MONOMER.
Family and domain databases
HAMAP	MF_01417. SpeA. [Tree]
InterPro	IPR009006. Ala_racemase/Decarboxylase_C. IPR002985. Arg_decrbxlase. IPR022643. De-COase2_C. IPR022644. De-COase2_N. IPR022653. De-COase2_pyr-phos_BS. IPR000183. Orn/DAP/Arg_de-COase. [Graphical view]
Gene3D	G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits.
KO	K01585.
PANTHER	PTHR11482:SF3. Arg_decrbxlase. 1 hit.
Pfam	PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view]
PIRSF	PIRSF001336. Arg_decrbxlase. 1 hit.
PRINTS	PR01180. ARGDCRBXLASE. PR01179. ODADCRBXLASE.
SUPFAM	SSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMs	TIGR01273. SpeA. 1 hit.
PROSITE	PS00878. ODR_DC_2_1. 1 hit. PS00879. ODR_DC_2_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPEA2_SYNY3

Accession

Primary (citable) accession number: P72587

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program