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Entry: A6BF67_9FIRM
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ID   A6BF67_9FIRM            Unreviewed;       499 AA.
AC   A6BF67;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
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   ECO:0000313|EMBL:EDM63654.1};
GN   ORFNames=DORLON_00938 {ECO:0000313|EMBL:EDM63654.1};
OS   Dorea longicatena DSM 13814.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=411462 {ECO:0000313|EMBL:EDM63654.1, ECO:0000313|Proteomes:UP000004016};
RN   [1] {ECO:0000313|EMBL:EDM63654.1, ECO:0000313|Proteomes:UP000004016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13814 {ECO:0000313|EMBL:EDM63654.1,
RC   ECO:0000313|Proteomes:UP000004016};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDM63654.1, ECO:0000313|Proteomes:UP000004016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13814 {ECO:0000313|EMBL:EDM63654.1,
RC   ECO:0000313|Proteomes:UP000004016};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Dorea longicatena (DSM 13814).";
RL   Submitted (APR-2007) 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:EDM63654.1}.
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DR   EMBL; AAXB02000003; EDM63654.1; -; Genomic_DNA.
DR   RefSeq; WP_006428759.1; NZ_DS264418.1.
DR   AlphaFoldDB; A6BF67; -.
DR   eggNOG; COG2160; Bacteria.
DR   HOGENOM; CLU_045663_0_0_9; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000004016; 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          365..477
FT                   /note="L-arabinose isomerase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11762"
FT   BINDING         306
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT   BINDING         335
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT   BINDING         451
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   499 AA;  56537 MW;  7FEA4190B9E10FBC CRC64;
     MLKTKNYQFW FCTGSQDLYG DECLAHVAEH SKIIVDALNK SGNLPYEVVW KPTMITNEVI
     RKTFNEANTD ENCAGVITWM HTFSPAKSWI LGLQEYRKPL LHLHTQFNRE IPYDTIDMDF
     MNENQAAHGD REYGHIFSRL NMERKVVAGY WEDEDVQKQI GSWMRTAVGV VESSHVRVMR
     VADNMRNVAV TEGDKVEAQI KFGWEVDAYP VNEVVEAVNA VSQADIDTLV EEYYDKYDIL
     LEGRDEKEFR EHVAVQAGIE LGFERFLDEN NYQAVVTHFG DLGGLKQLPG LAMQRLMEKG
     YGFGAEGDWK TAAMVRVMKI MTQGMKDAKG TSFMEDYTYN LVSGKEGVLE AHMLEVCPTI
     ADGKISIKEQ PLSMGNREDP ARLVFTSKTG PAIATSLIDL GDRFRLIIND VDCKKTEKPM
     PKLPVATAFW TPQPNLKVGT EAWILAGGAH HTAFSYDLTA EQMGDWAACM GIEAVYIDKD
     TTIRQFKNEL LWNSVAYRK
//
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