ID K9EEE5_9BACE Unreviewed; 502 AA.
AC K9EEE5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=HMPREF9447_03622 {ECO:0000313|EMBL:EKU89297.1};
OS Bacteroides oleiciplenus YIT 12058.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=742727 {ECO:0000313|EMBL:EKU89297.1, ECO:0000313|Proteomes:UP000009872};
RN [1] {ECO:0000313|EMBL:EKU89297.1, ECO:0000313|Proteomes:UP000009872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12058 {ECO:0000313|EMBL:EKU89297.1,
RC ECO:0000313|Proteomes:UP000009872};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., 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 oleiciplenus YIT 12058.";
RL Submitted (SEP-2012) 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:EKU89297.1}.
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DR EMBL; ADLF01000015; EKU89297.1; -; Genomic_DNA.
DR RefSeq; WP_009131149.1; NZ_JH992943.1.
DR AlphaFoldDB; K9EEE5; -.
DR STRING; 742727.HMPREF9447_03622; -.
DR PATRIC; fig|742727.4.peg.3692; -.
DR eggNOG; COG2160; Bacteria.
DR HOGENOM; CLU_045663_0_0_10; -.
DR OrthoDB; 9765600at2; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000009872; 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 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; 56378 MW; 29FA21FC3549BA2A CRC64;
MNAFDQYEVW FVTGAQLLYG GDAVIAVDAH SNEMVAGLNA SGNLPVKVVY KGTVNSSKEV
TAAFKAANND EKCIGVITWM HTFSPAKMWI HGLQELKKPL LHFHTQFNKE IPWDTMDMDF
MNLNQSAHGD REFGHIVTRM RKNRKVVVGH WQDEKAQGQI AAWMRVCAGW ADAQDMLIIR
FGDQMNNVAV TDGDKVSAEQ VLGYHVDYCP VNDLMKYYNA VEDKDVQAMV DTYFKEYDHA
PELEKAGTEA YVKVWNSAKA EIALRRILKD TGAKAFTTNF NDLGDFDQIP GLASQRLMEE
GYGFGAEGDW KTAALYRTTW FMSQGMPKGC SFLEDYTLHF DGEKSAILQA HMLEVCPLIA
EAKPKLEVHR LSIGIDSETA RLVFTSKQGE GVAATIVDLG NRFRLIVNKV ECIKSKPLPK
LPVASALWIP QPNLEVGAAA WILAGGTHHT SFSYDLTVEY WEDYAEMAGI EMVVIDENTT
ISEFKKELRM NEVYYMLNKA LC
//
