ARAA_YERE8
ID ARAA_YERE8 Reviewed; 500 AA.
AC A1JMB6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=YE2001;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12079.1; -; Genomic_DNA.
DR RefSeq; WP_011816285.1; NC_008800.1.
DR RefSeq; YP_001006253.1; NC_008800.1.
DR AlphaFoldDB; A1JMB6; -.
DR SMR; A1JMB6; -.
DR STRING; 393305.YE2001; -.
DR EnsemblBacteria; CAL12079; CAL12079; YE2001.
DR KEGG; yen:YE2001; -.
DR PATRIC; fig|393305.7.peg.2163; -.
DR eggNOG; COG2160; Bacteria.
DR HOGENOM; CLU_045663_0_0_6; -.
DR OMA; HMLEICP; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000000642; 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_0000312623"
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; 55700 MW; 522196C3FB130F8D CRC64;
MDVFKQSEVW FVIGSQNLYG PKTLQQVMDN AHHVVNSLNS EAGLPVKLVL KPLVTTPDEI
TALCREANYD TACIGVMTWL HTFSPAKMWI GGLSILHKPL LQFHTQFNAQ IPWETMDMDF
MNLNQTAHGG REFGFIGARM RQQHSVITGH WQDKEAHQRI SQWMRVAAAK QENQQLKVAR
FGDNMREVAV TEGDKVAAQI QFGYSVNAYG IGDLVTVVDA VSKGEIDALV EEYEATYRLT
DAVQLHGNKR ENLLDAARIE LGMKRFLEQG GFKAFTTNFE NLYGLKQLPG LAVQRLMQQG
YGFGGEGDWK TAALLRILKV MGTGLKGGTS FMEDYTYNFQ PGNDLVVGSH MLEVCPSIAK
EEKPLLDVQH LGIGGKADPA RLIFSTPAGP ALNASLIDMG NRFRLLVNVV DTVEQPHPLP
KLPVARAIWQ AQPSLATAAE AWIIAGGAHH TVFSQAIGVD ELRLYAEMHG IEFLLIDNDT
TLPAFKNEIR WNEVYYHLNR