Q03HQ0 (ARAA_PEDPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-arabinose isomerase
EC=5.3.1.4

Gene names

Name:	araA
Ordered Locus Names:	PEPE_0165

Organism

Pediococcus pentosaceus (strain ATCC 25745 / 183-1w) [Complete proteome] [HAMAP]

Taxonomic identifier

278197 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Pediococcus

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of L-arabinose to L-ribulose By similarity. HAMAP MF_00519
Catalytic activity	L-arabinose = L-ribulose. HAMAP MF_00519
Cofactor	Binds 1 manganese ion per subunit By similarity. HAMAP MF_00519
Pathway	Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. HAMAP MF_00519
Sequence similarities	Belongs to the arabinose isomerase family.

Ontologies

Keywords
Biological process	Arabinose catabolism Carbohydrate metabolism
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arabinose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW fucose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	L-arabinose isomerase activity Inferred from electronic annotation. Source: EC L-fucose isomerase activity Inferred from electronic annotation. Source: InterPro 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 – 474	474	L-arabinose isomerase HAMAP MF_00519		PRO_0000312615
Sites
	Metal binding	306	1	Manganese By similarity
	Metal binding	331	1	Manganese By similarity
	Metal binding	348	1	Manganese By similarity
	Metal binding	447	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03HQ0 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 200969A743A27800	FASTA	474	54,056
	10 20 30 40 50 60 MKKVQDYEFW FVTGSQFLYG EETLRSVEKD AKEIVDKLNE SKKLPYPVKF KLVATTAENI 70 80 90 100 110 120 TEVMKEVNYN DKVAGVITWM HTFSPAKNWI RGTELLQKPL LHLATQFLNH IPYDTIDFDY 130 140 150 160 170 180 MNLNQSAHGD REYAFINARL RKNNKIISGY WGDEGIQKQI AKWMDVAVAY NESYGIKVVT 190 200 210 220 230 240 FADKMRNVAV TDGDKIEAQI KFGWTVDYWG VADLVEEVNA VSDEDIDKKY EEMKNDYNFV 250 260 270 280 290 300 EGQNSSEKFE HNTKYQIREY FGLKKFMDDR GYTAFTTNFE DLAGLEQLPG LAAQMLMAEG 310 320 330 340 350 360 YGFAGEGDWK TAALDRLLKI MAHNKQTVFM EDYTLDLREG HEAILGSHML EVDPSIASDT 370 380 390 400 410 420 PRVEVHPLDI GGKEDPARFV FTGMEGDAVD VTMADYGDEF KLMSYDVTGN KTEKETPYLP 430 440 450 460 470 VAKQLWTPKQ GWKQGAEGWL TLGGGHHTVL SFAIDAEQLQ DLSNMFGLTY VNIK

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25745 / 183-1w.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000422 Genomic DNA. Translation: ABJ67272.1.
RefSeq	YP_803714.1. NC_008525.1.
3D structure databases
ProteinModelPortal	Q03HQ0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03HQ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4418644.
GenomeReviews	Gene locus PEPE_0165 in contig CP000422_GR.
KEGG	ppe:PEPE_0165.
NMPDR	fig|278197.10.peg.148.
PATRIC	22873682. VBIPedPen34213_0158.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2160.
HOGENOM	HBG297198.
OMA	DVAVAYN.
PhylomeDB	Q03HQ0.
ProtClustDB	PRK02929.
Enzyme and pathway databases
BioCyc	PPEN278197:PEPE_0165-MONOMER.
Family and domain databases
HAMAP	MF_00519. Arabinose_Isome. [Tree]
InterPro	IPR024664. Ara_Isoase_C. IPR004216. Fuc/Ara_isomerase_C. IPR009015. Fucose_isomerase_N/cen. IPR003762. Lara_isomerase. [Graphical view]
Pfam	PF11762. Arabinose_Iso_C. 1 hit. PF02610. Arabinose_Isome. 1 hit. [Graphical view]
PIRSF	PIRSF001478. L-ara_isomerase. 1 hit.
ProDom	PD018364. Lara_isomerase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF50443. Fuc_isomerase_C. 1 hit. SSF53743. Fuc_isomerase_N. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARAA_PEDPA

Accession

Primary (citable) accession number: Q03HQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program