ARAA_SALTY
ID ARAA_SALTY Reviewed; 500 AA.
AC P06189;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=STM0102;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=3891513; DOI=10.1016/0378-1119(85)90302-6;
RA Lin H.-C., Lei S.-P., Wilcox G.;
RT "The araBAD operon of Salmonella typhimurium LT2. II. Nucleotide sequence
RT of araA and primary structure of its product, L-arabinose isomerase.";
RL Gene 34:123-128(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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 -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00519}.
CC -!- PTM: The N-terminus is probably modified.
CC -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
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DR EMBL; M11047; AAA27024.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19066.1; -; Genomic_DNA.
DR PIR; A24985; ISEBAB.
DR RefSeq; NP_459107.1; NC_003197.2.
DR RefSeq; WP_000151691.1; NC_003197.2.
DR AlphaFoldDB; P06189; -.
DR SMR; P06189; -.
DR STRING; 99287.STM0102; -.
DR PaxDb; P06189; -.
DR EnsemblBacteria; AAL19066; AAL19066; STM0102.
DR GeneID; 1251620; -.
DR KEGG; stm:STM0102; -.
DR PATRIC; fig|99287.12.peg.105; -.
DR HOGENOM; CLU_045663_0_0_6; -.
DR OMA; HMLEICP; -.
DR PhylomeDB; P06189; -.
DR BioCyc; SENT99287:STM0102-MON; -.
DR BRENDA; 5.3.1.4; 5542.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008733; F:L-arabinose isomerase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IBA:GO_Central.
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..500
FT /note="L-arabinose isomerase"
FT /id="PRO_0000198393"
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"
FT CONFLICT 258
FT /note="R -> G (in Ref. 1; AAA27024)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="A -> R (in Ref. 1; AAA27024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 55892 MW; 97112E535F7EC2BF CRC64;
MTIFDNYEVW FVIGSQHLYG AETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTSPDEI
TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLSILNKPL LQFHTQFNAA LPWDSIDMDF
MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKEAHTRI GAWMRQAVSK QDTRQLKVCR
FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS IGDGDINALI 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
HLPAFKDALR WNEVYYGFKR
