ID   ARAA_SALPA              Reviewed;         500 AA.
AC   Q5PDF2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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}; OrderedLocusNames=SPA0104;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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   -!- 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; CP000026; AAV76137.1; -; Genomic_DNA.
DR   RefSeq; WP_000151699.1; NC_006511.1.
DR   AlphaFoldDB; Q5PDF2; -.
DR   SMR; Q5PDF2; -.
DR   EnsemblBacteria; AAV76137; AAV76137; SPA0104.
DR   KEGG; spt:SPA0104; -.
DR   HOGENOM; CLU_045663_0_0_6; -.
DR   OMA; HMLEICP; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000008185; 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.
FT   CHAIN           1..500
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_0000259342"
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;  55850 MW;  9714149D7517C942 CRC64;
     MTIFDNYEVW FVIGSQHLYG AETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTSPDEI
     TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLSILNKPL LQFHTQFNAA LPWDSIDMDF
     MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKEAHTRI GAWMRQAVSK QDTRQLKVCR
     FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS IGDGDISALI DEYESSYTLT
     PATQIHGDKR QNVREAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
     YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV
     EEKPILDVQH LGIGGKEDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
     KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALDLN DMRQFAEIHD IEIAVIDNDT
     RLPAFKDALR WNEVYYGLKR