C2GTB8 (C2GTB8_BIFLN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
L-arabinose isomerase HAMAP MF_00519
EC=5.3.1.4 HAMAP MF_00519

Gene names

Name:	araA HAMAP MF_00519 EMBL EEI81797.1
ORF Names:	HMPREF0175_0265 EMBL EEI81797.1

Organism

Bifidobacterium longum subsp. longum ATCC 55813 EMBL EEI81797.1

Taxonomic identifier

548480 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	505 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 SAAS SAAS003762
Catalytic activity	L-arabinose = L-ribulose. HAMAP MF_00519 SAAS SAAS003762
Cofactor	Binds 1 manganese ion per subunit By similarity. HAMAP MF_00519 SAAS SAAS003762
Pathway	Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. HAMAP MF_00519 SAAS SAAS003762
Sequence similarities	Belongs to the arabinose isomerase family. HAMAP MF_00519
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Ontologies

Keywords
Biological process	Arabinose catabolism HAMAP MF_00519 SAAS SAAS003762 Carbohydrate metabolism
Ligand	Manganese HAMAP MF_00519 SAAS SAAS003762 Metal-binding HAMAP MF_00519 SAAS SAAS003762
Molecular function	Isomerase HAMAP MF_00519 SAAS SAAS003762 EMBL EEI81797.1
Gene Ontology (GO)
Biological process	arabinose catabolic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP L-fucose isomerase activity Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	308	1	Manganese By similarity HAMAP MF_00519
	Metal binding	335	1	Manganese By similarity HAMAP MF_00519
	Metal binding	352	1	Manganese By similarity HAMAP MF_00519
	Metal binding	453	1	Manganese By similarity HAMAP MF_00519

Sequences

	Sequence		Length	Mass (Da)
	C2GTB8 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: 7665BFB00AD37E4C	FASTA	505	55,868
	10 20 30 40 50 60 MVMENPFEGK EIWFGVGSQD LYGEEALRQV AIHSAEMVDY LNNTGKIPAK IVLKPTLKSS 70 80 90 100 110 120 DGVKEFMVEA SANPNVIGVI TWCHTFSPAK MWIRGLEVLT KPLLQLATQH HKEIPWETID 130 140 150 160 170 180 MDFMNLNQAA HGDREFGYIV SRLGIKRKVV VGHYTDPEVA EKLGTWARAC AGWDASNNMK 190 200 210 220 230 240 VMRWGDNMRN VAVTEGDKTE AERVFGASIN TWAVNELVAA YDAVKDDQVK EIIEDYKAKY 250 260 270 280 290 300 DVDPALLDAK YDSLFIAAKE EAAMVNMMRA NGCTAGVDNF EDLGALPQLP GVGPQRFPSE 310 320 330 340 350 360 YGWGFSAEGD WKTAVLVRIG AVMGYGLEGG ASLMEDYSYN FTEGDELDMG SHMLEVSPSI 370 380 390 400 410 420 GTIAKPKLEI HPLGIGGKAD PVRLVFSGKP AKDAVVVSMS DVRERFRLLM DVVDVVEPQG 430 440 450 460 470 480 SLKELPCARA VWEPKPSLKT AVECWITAGG SHHTCMTTSV GREAWEDFAR IAGVELAVID 490 500 ENTTARQFEK ELELSEMYHR LNNQH

References

[1]

Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. , Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., Worley K., Gibbs R. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 55813 EMBL EEI81797.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACHI01000005 Genomic DNA. Translation: EEI81797.1.
3D structure databases
ProteinModelPortal	C2GTB8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	36945262. VBIBifLon7869_1881.
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

C2GTB8_BIFLN

Accession

Primary (citable) accession number: C2GTB8

Entry history

Integrated into UniProtKB/TrEMBL:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	January 25, 2012
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)