Q0ACK8 (SPEA_ALHEH) 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:	Mlg_0072

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	628 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
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.

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: 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 – 628	628	Biosynthetic arginine decarboxylase HAMAP MF_01417		PRO_1000024253
Regions
	Region	281 – 291	11	Substrate-binding Potential
Amino acid modifications
	Modified residue	101	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0ACK8 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 984DD1693C8BB682	FASTA	628	69,264
	10 20 30 40 50 60 MSDWSIGLAR QVWSVQHWSG GYFDISDEGR VVARPDRDPA RAPLDLAGIA AEARHQGLGL 70 80 90 100 110 120 PVLVRFLDIL HDRVDSLCQA FRQAMVEDGY RGGYRAVYPI KVNQQRRVVE EIIRHGNGRV 130 140 150 160 170 180 GLEAGSKPEL MAVLALTPPG GTVVCNGYKD REYVRLALRG RQLGLQVHLV IEKASELELV 190 200 210 220 230 240 LEEAAALGVT PSLGMRVRLA TIGAGKWQNT GGEKSKFGLT AAQALAVVDR LRAAGCLDWL 250 260 270 280 290 300 RLLHFHLGSQ IPNIRDIRRG MREAARYYAE LRALGAPVET VDVGGGLGVD YEGSRSRSFC 310 320 330 340 350 360 SMNYTVAEYA HNVVHALWQV CEDEGLPHPD IITESGRAMT AHHAVLITDV IDGDRVPGGA 370 380 390 400 410 420 DLLAPADAAP RVLHELWTVW TGLDRRHPLE AYHDAAHGLA EAQELYAHGV LNLTDRARAE 430 440 450 460 470 480 RIWQAVCHAL LQRLDPRRRP HRELLDELNE KLADKLFCNF SLFQSMPDVW AIDQIFPVLP 490 500 510 520 530 540 LQRLDEPPAS RAVLQDLTCD SDGCIRGYVD RDGVESTLPL PPWRPGEPYL LGIFLVGAYQ 550 560 570 580 590 600 EILGDMHNLF GDTHSVNVRL TGEGYALSGA AHGDTITDVL RYVDFDAEVL RGIYRERVVA 610 620 AAGLDATARA QCLADLEAGL RGYTYLDT

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." 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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MLHE-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI55429.1.
RefSeq	YP_740919.1. NC_008340.1.
3D structure databases
ProteinModelPortal	Q0ACK8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0ACK8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4270350.
GenomeReviews	Gene locus Mlg_0072 in contig CP000453_GR.
KEGG	aeh:Mlg_0072.
NMPDR	fig|187272.6.peg.68.
PATRIC	20859316. VBIAlkEhr114327_0073.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1166.
HOGENOM	HBG321436.
OMA	LICNGYK.
PhylomeDB	Q0ACK8.
ProtClustDB	PRK05354.
Enzyme and pathway databases
BioCyc	AEHR187272:MLG_0072-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_ALHEH

Accession

Primary (citable) accession number: Q0ACK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program