ARAA_BIFLO
ID ARAA_BIFLO Reviewed; 505 AA.
AC Q8G7J3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=L-arabinose isomerase {ECO:0000255|HAMAP-Rule:MF_00519};
DE EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519};
GN Name=araA {ECO:0000255|HAMAP-Rule:MF_00519}; OrderedLocusNames=BL0272;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-arabinopyranose = L-ribulose; Xref=Rhea:RHEA:14821,
CC ChEBI:CHEBI:16880, ChEBI:CHEBI:40886; EC=5.3.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00519};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 1/3. {ECO:0000255|HAMAP-Rule:MF_00519}.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
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DR EMBL; AE014295; AAN24113.1; -; Genomic_DNA.
DR RefSeq; NP_695477.1; NC_004307.2.
DR RefSeq; WP_007051388.1; NC_004307.2.
DR AlphaFoldDB; Q8G7J3; -.
DR SMR; Q8G7J3; -.
DR STRING; 206672.BL0272; -.
DR EnsemblBacteria; AAN24113; AAN24113; BL0272.
DR GeneID; 66504583; -.
DR KEGG; blo:BL0272; -.
DR PATRIC; fig|206672.9.peg.1008; -.
DR HOGENOM; CLU_045663_0_0_11; -.
DR OMA; HMLEICP; -.
DR PhylomeDB; Q8G7J3; -.
DR BRENDA; 5.3.1.4; 851.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008733; F:L-arabinose isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10940; -; 1.
DR HAMAP; MF_00519; Arabinose_Isome; 1.
DR InterPro; IPR024664; Ara_Isoase_C.
DR InterPro; IPR038583; AraA_N_sf.
DR InterPro; IPR004216; Fuc/Ara_isomerase_C.
DR InterPro; IPR009015; Fucose_isomerase_N/cen_sf.
DR InterPro; IPR003762; Lara_isomerase.
DR PANTHER; PTHR38464; PTHR38464; 1.
DR Pfam; PF11762; Arabinose_Iso_C; 1.
DR Pfam; PF02610; Arabinose_Isome; 1.
DR PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR SUPFAM; SSF50443; SSF50443; 1.
DR SUPFAM; SSF53743; SSF53743; 1.
PE 3: Inferred from homology;
KW Arabinose catabolism; Carbohydrate metabolism; Isomerase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..505
FT /note="L-arabinose isomerase"
FT /id="PRO_0000312604"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 453
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ SEQUENCE 505 AA; 55868 MW; 7665BFB00AD37E4C CRC64;
MVMENPFEGK EIWFGVGSQD LYGEEALRQV AIHSAEMVDY LNNTGKIPAK IVLKPTLKSS
DGVKEFMVEA SANPNVIGVI TWCHTFSPAK MWIRGLEVLT KPLLQLATQH HKEIPWETID
MDFMNLNQAA HGDREFGYIV SRLGIKRKVV VGHYTDPEVA EKLGTWARAC AGWDASNNMK
VMRWGDNMRN VAVTEGDKTE AERVFGASIN TWAVNELVAA YDAVKDDQVK EIIEDYKAKY
DVDPALLDAK YDSLFIAAKE EAAMVNMMRA NGCTAGVDNF EDLGALPQLP GVGPQRFPSE
YGWGFSAEGD WKTAVLVRIG AVMGYGLEGG ASLMEDYSYN FTEGDELDMG SHMLEVSPSI
GTIAKPKLEI HPLGIGGKAD PVRLVFSGKP AKDAVVVSMS DVRERFRLLM DVVDVVEPQG
SLKELPCARA VWEPKPSLKT AVECWITAGG SHHTCMTTSV GREAWEDFAR IAGVELAVID
ENTTARQFEK ELELSEMYHR LNNQH