ID   ARAA1_CLOAB             Reviewed;         488 AA.
AC   Q97JE4;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=L-arabinose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00519};
DE            EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519};
GN   Name=araA1 {ECO:0000255|HAMAP-Rule:MF_00519}; OrderedLocusNames=CA_C1342;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79310.1; -; Genomic_DNA.
DR   PIR; C97065; C97065.
DR   RefSeq; NP_347970.1; NC_003030.1.
DR   RefSeq; WP_010964651.1; NC_003030.1.
DR   AlphaFoldDB; Q97JE4; -.
DR   SMR; Q97JE4; -.
DR   STRING; 272562.CA_C1342; -.
DR   EnsemblBacteria; AAK79310; AAK79310; CA_C1342.
DR   GeneID; 44997847; -.
DR   KEGG; cac:CA_C1342; -.
DR   PATRIC; fig|272562.8.peg.1547; -.
DR   eggNOG; COG2160; Bacteria.
DR   HOGENOM; CLU_045663_0_0_9; -.
DR   OMA; HMLEICP; -.
DR   OrthoDB; 507566at2; -.
DR   BRENDA; 5.3.1.4; 1452.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000000814; 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..488
FT                   /note="L-arabinose isomerase 1"
FT                   /id="PRO_0000198383"
FT   BINDING         306
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         331
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         348
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         447
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   488 AA;  55206 MW;  1AFBFA04E75183D1 CRC64;
     MLKNKKLEFW FVVGSQNLYG EEALNAVKKD SKEIVDSLNE SGKLPYPIVF KTLATSADEI
     KNIVKEINYR DEVAGVITWM HTFSPAKMWI AGTKLLQKPL LHLATQFNEN IPWKTIDMDY
     MNLHQSAHGD REYGFINARL NKNNKVVVGY WKDNQVQKEI AEWMQVAYGY VASENIKVAR
     FGDNMRNVAV TEGDKVEAQI QFGWTVDYFA IGDLVAEMNK VSQKDIDATY EEFKDIYILD
     IGDNDPEFYE NHVKEQIKIE IGLRNFLEAG NYTAFTTNFE DLYGMKQLPG LAVQRLNAEG
     YGFAGEGDWK TAALNRLFKI MTDNKKTGFM EDYTYELSAG NERILGAHML EVDPTLAASK
     PRVVVKPLGI GDKEAPARLI FDGVVGDGVV VSMLDLGTHY RLLINEVKAV KPTEDAPNLP
     VAKLVWQPQP NFKDAVKAWI YAGGGHHTVA TLELTVEQVY DWSRMVGLET IVIDHNTNLR
     DIIKETSR