ID E5X1Z4_9BACE Unreviewed; 502 AA.
AC E5X1Z4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=HMPREF1016_03059 {ECO:0000313|EMBL:EFV28718.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV28718.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV28718.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV28718.1,
RC ECO:0000313|Proteomes:UP000003246};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL Submitted (OCT-2010) 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:EFV28718.1}.
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DR EMBL; ACWG01000039; EFV28718.1; -; Genomic_DNA.
DR RefSeq; WP_004294896.1; NZ_GL622546.1.
DR AlphaFoldDB; E5X1Z4; -.
DR HOGENOM; CLU_045663_0_0_10; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000003246; 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 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 363..475
FT /note="L-arabinose isomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11762"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 334
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 449
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
SQ SEQUENCE 502 AA; 56336 MW; 6AF13D877B5F412A CRC64;
MNAFDQYEVW FVTGAQLLYG GDAVVAVDAH SNEMVKGLND SGRLPVKIVY KGTVNSSKEV
TAAFKAANND EKCIGVITWM HTFSPAKMWI HGLQELKKPL LHFHTQFNKE IPWDTMDMDF
MNLNQSAHGD REFGHIVTRM RKNRKVVVGH WQDEKAQKQI ASWMRVAAAW ADAQDMLIIR
FGDQMNNVAV TDGDKVSAEQ VLGYHVDYYP INDVMTYYNA VDDADVKALV AEYFKLYDHD
AALEKEGTEA YTKVWNSAKA EIAIRRVLKD TGAKGFTTNF NDLGDFDQIP GLASQRLMAE
GYGFGAEGDW KTAALYRTTW FMSQGMPNGC SFLEDYTLNF DGEKSAILQA HMLEVCPLIA
EQKPKLEVHR LSIGIDSETA RLVFTSKQGK GVAATIVDLG NRFRLIVNKV ECIKSKPLPK
LPVASALWIP MPNLEVGAAA WILAGGTHHT SFSYDLTVED WGDFAEMAGI EMIVIDENTT
ISEFKKELRM NEVYYMLNKA LC
//
