ID   ARAA_CITK8              Reviewed;         500 AA.
AC   A8ALP0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   28-JAN-2026, entry version 88.
DE   RecName: Full=L-arabinose isomerase {ECO:0000255|HAMAP-Rule:MF_00519};
DE            EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519};
GN   Name=araA {ECO:0000255|HAMAP-Rule:MF_00519};
GN   OrderedLocusNames=CKO_03320;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC         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   -!- SUBUNIT: Homohexamer. {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; CP000822; ABV14403.1; -; Genomic_DNA.
DR   RefSeq; WP_012134106.1; NC_009792.1.
DR   AlphaFoldDB; A8ALP0; -.
DR   SMR; A8ALP0; -.
DR   STRING; 290338.CKO_03320; -.
DR   GeneID; 45137085; -.
DR   KEGG; cko:CKO_03320; -.
DR   HOGENOM; CLU_045663_0_0_6; -.
DR   OrthoDB; 9765600at2; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000008148; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 D-xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR   CDD; cd03557; L-arabinose_isomerase; 1.
DR   FunFam; 3.40.50.10940:FF:000001; 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; IPR055390; AraA_central.
DR   InterPro; IPR055389; AraA_N.
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   NCBIfam; NF002795; PRK02929.1; 1.
DR   PANTHER; PTHR38464; L-ARABINOSE ISOMERASE; 1.
DR   PANTHER; PTHR38464:SF1; L-ARABINOSE ISOMERASE; 1.
DR   Pfam; PF24856; AraA_central; 1.
DR   Pfam; PF02610; AraA_N; 1.
DR   Pfam; PF11762; Arabinose_Iso_C; 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; Carbohydrate metabolism; Isomerase; Manganese;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..500
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_1000050906"
FT   BINDING         306
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         333
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         350
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         450
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   500 AA;  55897 MW;  ED94BF99B5B5E527 CRC64;
     MTIFDNYEVW FVIGSQHLYG SETLRQVTQH AEHVVKALNT EAKLPCKLVL KPLGTSPDEI
     TAICRDASYD DRCAGLVVWL HTFSPAKMWI NGLSILNKPL LQFHTQFNAA LPWDSIDMDF
     MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKHAHARI GSWMRQAVSR QDTRHLKVCR
     FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNA VSDGDINALV DEYESHYTLT
     PATQIHGDKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
     YGFAGEGDWK TAALLRIMKV MSGGLPGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV
     EEKPILDVQH LGIGGKDAPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHDLP
     KLPVANALWK AQPDLTIASE AWILAGGAHH TVFSHALDLN DMRQFAEMHD IEITVIDNDT
     RLPAFKDALR WNEVYYGFKR
//