A5GB52 (SPEA_GEOUR) 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:	Gura_0983

Organism

Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens) [Complete proteome] [HAMAP]

Taxonomic identifier

351605 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter › Geobacter uraniireducens

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP-Rule MF_01417
Catalytic activity	L-arginine = agmatine + CO2. HAMAP-Rule MF_01417
Cofactor	Magnesium By similarity. Pyridoxal phosphate By similarity.
Pathway	Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule 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
Gene Ontology (GO)
Biological_process	arginine catabolic process Inferred from electronic annotation. Source: InterPro spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	arginine decarboxylase activity Inferred from electronic annotation. Source: HAMAP 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 – 635	635	Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417		PRO_1000087404
Regions
	Region	282 – 292	11	Substrate-binding Potential
Amino acid modifications
	Modified residue	100	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5GB52 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 7CE13746E2FB8758	FASTA	635	71,778
	10 20 30 40 50 60 MERWSINDSA KIYNLNNWGA DLFSINKKGN VCVHPSSNSK HSIDLRALVD DLIKRKIKPP 70 80 90 100 110 120 ILLRFMDVLQ GRIASINRVF KNAIQENNYP AKYQTFYPIK VNQQRQVVEA IANFGKRYNI 130 140 150 160 170 180 GLEVGSKPEL VAGISFATGN NLPIICNGYK DTEYIEMVLS ATKIGYDITL VVEKLFELEK 190 200 210 220 230 240 IIELVKKTGV QPKLGIRVKL SSKGIGKWAT SGGEDAKFGL RMSEIIAAIE MLEKHDLIKC 250 260 270 280 290 300 VKLLHFHIGS QITKIDKIKT ALIEGARIYA EMRKLGVGIE YLDIGGGLGV DYDGSKSSNF 310 320 330 340 350 360 SSVNYSIEEY ANDVIYQIKN ICEDAGVECP NIISESGRAT VAHYSVLVTN VLNTNTQNIM 370 380 390 400 410 420 PDFEATLNEA EKLAPTVKKL EDIYKSIDRY SLREDYHDTL QLIQEAVSLF NLGYLTLNDR 430 440 450 460 470 480 AMAEWLYGKI IRKINSIVEK IKPIPEELQN FQLSLRQTYF ANFSLFQSVP DSWAIDQLFP 490 500 510 520 530 540 IVPIQRLNQK PDVIASIADI TCDSDGEITS FVGENGRTKF LPLHKIRKDE AYYIGFFLIG 550 560 570 580 590 600 AYQEILGDMH NLFGDTNAVH ITFNKKTGYI IDTVINGDAT WESLKYVQYK GPEILKRVRD 610 620 630 NLEKDVALRK ISIEESSHFL ELLDRTLLGY TYLGE

References

[1]

"Complete sequence of Geobacter uraniireducens Rf4." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., Lovley D., Richardson P. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Rf4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000698 Genomic DNA. Translation: ABQ25189.1.
RefSeq	YP_001229762.1. NC_009483.1.
3D structure databases
ProteinModelPortal	A5GB52.
ModBase	Search...
Protein-protein interaction databases
STRING	351605.Gura_0983.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABQ25189; ABQ25189; Gura_0983.
GeneID	5163174.
KEGG	gur:Gura_0983.
PATRIC	22031920. VBIGeoUra13052_1053.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1166.
HOGENOM	HOG000029191.
KO	K01585.
OMA	MIHFHIG.
ProtClustDB	PRK05354.
Enzyme and pathway databases
BioCyc	GURA351605:GI6A-1041-MONOMER.
UniPathway	UPA00186; UER00284.
Family and domain databases
HAMAP	MF_01417. SpeA.
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]
PANTHER	PTHR11482:SF3. PTHR11482:SF3. 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_GEOUR

Accession

Primary (citable) accession number: A5GB52

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 12, 2007
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program