ARAA_SHESW
ID ARAA_SHESW Reviewed; 500 AA.
AC A1RJD6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
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};
GN OrderedLocusNames=Sputw3181_1946;
OS Shewanella sp. (strain W3-18-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=351745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W3-18-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. W3-18-1.";
RL Submitted (DEC-2006) 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 -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00519}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM24781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000503; ABM24781.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041408176.1; NC_008750.1.
DR AlphaFoldDB; A1RJD6; -.
DR SMR; A1RJD6; -.
DR GeneID; 45042526; -.
DR KEGG; shw:Sputw3181_1946; -.
DR HOGENOM; CLU_045663_0_0_6; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000002597; 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_0000312620"
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 349
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT BINDING 448
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
SQ SEQUENCE 500 AA; 55640 MW; 44AB0CA45785A47B CRC64;
MKAFKQKQVW FVTGSQDLYG PKVLEQVAKN SEQIVNGFNQ SDAISMEVVY KPTVKSPREI
YAVCQAANSD ENCVGIILWM HTFSPAKMWI AGLNELSKPF MHLHTQFNAE LPWADINMNY
MNTHQSAHGC REFGYIGTRM RKERKVVVGH WQTNDVQAQV DDWCRAAAGW NESQNLRIAR
FGDNMRQVAV TEGDKVAAQI QFGYEVHAYS LGELNDAINA ISENDITAQI DRYASEYIIS
NELFNDEYQL DRLRKEAKIE LGLAQFLKDG EFGAFTNCFE NLTGMTGLPG LATQRLMANG
IGYGGEGDWK TAAMVRIMKV MGQGRVGGTS FMEDYTYNFG ATDQVLGAHM LEVCPSIAAS
KPRLEVHRHT IGVRCDVPRL LFTAKAGPAI NVSTIDLGNR FRIILNELDT VTPPQDLPNL
PVASALWEPR PNLSIAAAAW IHAGGAHHSA YSQAISTENI VDFAEMAGAE LVIIDADTQI
RQFKNELRQN SVYYGLARGL