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ARAA_YERPN
ID   ARAA_YERPN              Reviewed;         500 AA.
AC   Q1CIX9; C4GT18;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=YPN_1722;
GN   ORFNames=YP516_1913;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) 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; CP000305; ABG18051.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000009; EEO77178.1; -; Genomic_DNA.
DR   RefSeq; WP_002228461.1; NZ_ACNQ01000009.1.
DR   AlphaFoldDB; Q1CIX9; -.
DR   SMR; Q1CIX9; -.
DR   EnsemblBacteria; ABG18051; ABG18051; YPN_1722.
DR   KEGG; ypn:YPN_1722; -.
DR   HOGENOM; CLU_045663_0_0_6; -.
DR   OMA; HMLEICP; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000008936; 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_0000259348"
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;  55608 MW;  9E5C580E8E87A747 CRC64;
     MDVFKQSEVW FVIGSQNLYG PKTLQQVMDN AHQVVNSLNN EAGLPVKLVL KPLVTTPDEI
     TALCREANYD TACIGIMTWL HTFSPAKMWI GGLSILNKPL LQFHTQFNAQ IPWKTMDMDF
     MNLNHTAHGG REFGFIGARM RQQHSVITGH WQDKEAHQRI GQWMRVAAAK QESQQLKVAR
     FGDNMREVAV TEGDKVAAQI QFGYSVNAYG IGDLVAVVDA VSKGDIDTLV EEYEATYRFT
     DAVKLNGDKR ENLLDAARIE LGMTRFLEQG GFKAFTTNFE NLYGLKQLPG LAVQRLMQQG
     YGFGGEGDWK TAALLRILKV MGTGLKGGTS FMEDYTYNFQ PGNDLVVGSH MLEVCPSIAK
     EEKPLLDVQH LGIGGKADPA RLIFSTPAGP ALNASLIDMG NRFRLLVNVV DTVEQPHPLP
     KLPVARAIWQ AQPSLATAAE AWIIAGGAHH TVFSQAVGVD ELRLYAEMHG IEFLLIDNDT
     TLPAFKNEIR WNEVYYQLNR
 
 
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