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ARAA_SALAR
ID   ARAA_SALAR              Reviewed;         500 AA.
AC   A9MQF1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=SARI_02903;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-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;
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; CP000880; ABX22749.1; -; Genomic_DNA.
DR   RefSeq; WP_000151766.1; NC_010067.1.
DR   AlphaFoldDB; A9MQF1; -.
DR   SMR; A9MQF1; -.
DR   STRING; 41514.SARI_02903; -.
DR   EnsemblBacteria; ABX22749; ABX22749; SARI_02903.
DR   KEGG; ses:SARI_02903; -.
DR   HOGENOM; CLU_045663_0_0_6; -.
DR   OMA; HMLEICP; -.
DR   OrthoDB; 507566at2; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000002084; 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..500
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_1000081678"
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;  56030 MW;  6E219FF8558E76D7 CRC64;
     MTIFDNYEVW FVIGSQHLYG PKTLRQVTQH AEHVVKALNT EAKLPCKLVL KPLGTSPDEI
     TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLSILNKPL LQFHTQFNAA LPWDSIDMDF
     MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKEAHTRI SAWMRQAVSK QDIRQLKVCR
     FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDINALI DEYESSYTLT
     PATRIHGDKR QNVREAARIE LGIKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
     YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV
     EEKPLLDVQH LGIGGKEDPA RLIFNTQTGS AIVASLIDLG DRYRLLVNCI DTVKTPHDLP
     KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALDLN DMRQFAEMHD IEIAVIDNDT
     HLPGFKDALR WNDMYYSLKH
 
 
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