ARAA_BIFAA
ID ARAA_BIFAA Reviewed; 504 AA.
AC A1A3A8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=BAD_1410;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009256; BAF40191.1; -; Genomic_DNA.
DR RefSeq; WP_003809815.1; NC_008618.1.
DR AlphaFoldDB; A1A3A8; -.
DR SMR; A1A3A8; -.
DR STRING; 1680.BADO_1621; -.
DR EnsemblBacteria; BAF40191; BAF40191; BAD_1410.
DR GeneID; 56675634; -.
DR KEGG; bad:BAD_1410; -.
DR HOGENOM; CLU_045663_0_0_11; -.
DR OMA; HMLEICP; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000008702; 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..504
FT /note="L-arabinose isomerase"
FT /id="PRO_0000312603"
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 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ SEQUENCE 504 AA; 55884 MW; FD2E93AD90377119 CRC64;
MAMENPFEGK EIWFGVGSQD LYGEEALRQV AQQTGEMVDF LNATGKIPAK IVLKPTLKSS
DGVKAFMTEA SANPNVIGVI TWCHTFSPAK MWIRGLEVLT KPLLQLATQH HKEIPWETID
MDFMNLNQAA HGDREFGYIV SRLGIPRKIV VGHYTDPEVA EKVGTWARAC AGWDASQNMK
VMRWGDNMRN VAVTEGDKTE AERVFGASIN TWAVNDLVAA YEKVKDSQVK DLIEDYKAKY
DVAPELLDSR YDELFIAAKE EAAMVNMMRE NGCTAGVDNF EDLGTLPQLP GVGPQRFPSE
YGWGFSAEGD WKTSVLVRIG AVMGYGLEGG ASLMEDYSYN FVPGNEFDMG SHMLEVSPSI
GTIAKPKLAI YPLGIGGKSD PVRLVFSGKP ADAVVVSMAD ERERFRLLMD EVTIVEPQGS
LKNLPCARAV WKPKPDLKTA VQCWITAGGS HHTCMTTSVG REAWEDFARI AGVELAVIDE
NTNARQFEKE LELSEMYHRL NNRH