ID R9HBU3_BACT4 Unreviewed; 509 AA.
AC R9HBU3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=L-arabinose isomerase {ECO:0000256|HAMAP-Rule:MF_00519};
DE EC=5.3.1.4 {ECO:0000256|HAMAP-Rule:MF_00519};
GN Name=araA {ECO:0000256|HAMAP-Rule:MF_00519};
GN ORFNames=C799_01644 {ECO:0000313|EMBL:EOS01266.1};
OS Bacteroides thetaiotaomicron dnLKV9.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1235785 {ECO:0000313|EMBL:EOS01266.1, ECO:0000313|Proteomes:UP000014207};
RN [1] {ECO:0000313|EMBL:EOS01266.1, ECO:0000313|Proteomes:UP000014207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dnLKV9 {ECO:0000313|Proteomes:UP000014207};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides thetaiotaomicron dnLKV9.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00519};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00519};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00519}.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC {ECO:0000256|HAMAP-Rule:MF_00519}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS01266.1}.
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DR EMBL; ASSM01000008; EOS01266.1; -; Genomic_DNA.
DR RefSeq; WP_008760642.1; NZ_KE159459.1.
DR AlphaFoldDB; R9HBU3; -.
DR SMR; R9HBU3; -.
DR GeneID; 60926311; -.
DR PATRIC; fig|1235785.3.peg.1639; -.
DR HOGENOM; CLU_045663_0_0_10; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000014207; Unassembled WGS sequence.
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 CDD; cd03557; L-arabinose_isomerase; 1.
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; L-ARABINOSE ISOMERASE; 1.
DR PANTHER; PTHR38464:SF1; L-ARABINOSE ISOMERASE; 1.
DR Pfam; PF11762; Arabinose_Iso_C; 1.
DR Pfam; PF02610; Arabinose_Isome; 1.
DR PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR SUPFAM; SSF50443; FucI/AraA C-terminal domain-like; 1.
DR SUPFAM; SSF53743; FucI/AraA N-terminal and middle domains; 1.
PE 3: Inferred from homology;
KW Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935, ECO:0000256|HAMAP-
KW Rule:MF_00519};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00519};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00519};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00519};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00519}.
FT DOMAIN 369..482
FT /note="L-arabinose isomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11762"
FT BINDING 313
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 340
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 357
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 456
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
SQ SEQUENCE 509 AA; 57174 MW; DE04E4669834332C CRC64;
MNNVFDQYEV WFVTGAQLLY GGDAVIAVDA HSNEMVNGLN ESGKLPVKVV YKGTANSSKE
VEAVFKAANN DDKCVGVITW MHTFSPAKMW IHGLQQLKKP LLHLHTQFNK EIPWDTMDMD
FMNLNQSAHG DREFGHICTR MRIRRKVVVG YWKEEETLHK IAVWMRVCAG WADSQDMLII
RFGDQMNNVA VTDGDKVEAE QRMGYHVDYC PASELMEYHK DIKNADVDAL VATYFNDYDH
DASLEDKSTE AYQKVWNAAK AELALRAILK AKGAKGFTTN FDDLGQTDGS YFDQIPGLAS
QRLMAEGYGF GAEGDWKSAA LYRTVWVMNQ GLPKGCSFLE DYTLNFDGAN SSILQSHMLE
ICPLIAANKP RLEVHFLGIG IRKSQTARLV FTSKTGTGCT ATVVDMGNRF RLIVNDVECI
EPKPLPKLPV ASALWIPMPN LEVGAGAWIL AGGTHHSCFS YDLTAEYWED YAEIAGIEMV
HINKDTTISC FKKELRMNEV YYMLNKALC
//
