Q8DHY6 (SPEA_THEEB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	speA
Ordered Locus Names:	tll1807

Organism

Thermosynechococcus elongatus (strain BP-1)

Taxonomic identifier

197221 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length	637 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 – 637	637	Biosynthetic arginine decarboxylase HAMAP MF_01417		PRO_0000149979
Regions
	Region	289 – 299	11	Substrate-binding Potential
Amino acid modifications
	Modified residue	107	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8DHY6 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: A924C72CB50F29C5	FASTA	637	70,856
	10 20 30 40 50 60 MALTVTKTSN WTIEDSEQLY RIQGWGEPYF GINAAGHVTV SPKGDRGGSL DLYELVQALQ 70 80 90 100 110 120 QRNISLPLLL RFSDILEDRI ERLNACFARA IARYGYQGAY KGVFPIKCNQ QRHIIEALVR 130 140 150 160 170 180 FGQSHQFGLE AGSKPELLIA LAMLNTPGAL LICNGYKDRS YIETAILARR LGHTSIIVLE 190 200 210 220 230 240 QPEEVAEVIA VSQALGIEPI VGVRAKLSTQ GVGRWGTSAG DRAKFGLTVP EILTAVEQLR 250 260 270 280 290 300 AAGMLNALQL LHFHIGSQIS AISVIKDAIR EAGQIYGELV RLGANMQYLD VGGGLGVDYD 310 320 330 340 350 360 GSKTNFHASK NYSMQNYASD VVAGIKDACR QRGIPDPTLI SESGRAIASH QSVLIFNVLG 370 380 390 400 410 420 VSEVPKITPE PATAEEHLII RNLYDTYQAI DENNYQEAYN DALQFKGEAI SLFNFGYLSL 430 440 450 460 470 480 PERARAESLF WACCAKILGI ARQQEYVPDD LEDLEKIMAS IYYINLSVFQ SVPDSWAIDQ 490 500 510 520 530 540 LFPIMPIHRL DEEPTERGIL ADLTCDSDGK IDQFIDLRDV KSVLELHPFR PGEPYYLGLF 550 560 570 580 590 600 LNGAYQEIMG NLHNLFGDTN AVHIRLTPKG YEIEHLVRGD TMQEVLGYVQ YQGDALLEKI 610 620 630 RCRTEAALAE EQITLAEAQH LLENYERSLR SYTYLSS

References

[1]

"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1." Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. , Takeuchi C., Yamada M., Tabata S. DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BP-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000039 Genomic DNA. Translation: BAC09359.1.
RefSeq	NP_682597.1. NC_004113.1.
3D structure databases
ProteinModelPortal	Q8DHY6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8DHY6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1012401.
GenomeReviews	Gene locus tll1807 in contig BA000039_GR.
KEGG	tel:tll1807.
NMPDR	fig|197221.1.peg.1806.
PATRIC	23928998. VBITheElo119873_1889.
Phylogenomic databases
eggNOG	COG1166.
HOGENOM	HBG321436.
OMA	LICNGYK.
ProtClustDB	PRK05354.
Enzyme and pathway databases
BioCyc	TELO197221:TLL1807-MONOMER.
Family and domain databases
HAMAP	MF_01417. SpeA. [Tree]
InterPro	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. [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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SPEA_THEEB

Accession

Primary (citable) accession number: Q8DHY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program