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Database: UniProt
Entry: R5CQ22_9BACT
LinkDB: R5CQ22_9BACT
Original site: R5CQ22_9BACT 
ID   R5CQ22_9BACT            Unreviewed;       513 AA.
AC   R5CQ22;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=L-arabinose isomerase {ECO:0000256|HAMAP-Rule:MF_00519};
DE            EC=5.3.1.4 {ECO:0000256|HAMAP-Rule:MF_00519};
GN   Name=araA {ECO:0000256|HAMAP-Rule:MF_00519};
GN   ORFNames=BN567_01286 {ECO:0000313|EMBL:CCX70030.1};
OS   Prevotella sp. CAG:255.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262923 {ECO:0000313|EMBL:CCX70030.1, ECO:0000313|Proteomes:UP000017913};
RN   [1] {ECO:0000313|EMBL:CCX70030.1, ECO:0000313|Proteomes:UP000017913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:255 {ECO:0000313|Proteomes:UP000017913};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00519};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00519};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00519}.
CC   -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00519}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCX70030.1}.
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DR   EMBL; CAWV010000158; CCX70030.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5CQ22; -.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000017913; Unassembled WGS sequence.
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; L-ARABINOSE ISOMERASE; 1.
DR   PANTHER; PTHR38464:SF1; L-ARABINOSE ISOMERASE; 1.
DR   Pfam; PF11762; Arabinose_Iso_C; 1.
DR   Pfam; PF02610; Arabinose_Isome; 1.
DR   PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR   SUPFAM; SSF50443; FucI/AraA C-terminal domain-like; 1.
DR   SUPFAM; SSF53743; FucI/AraA N-terminal and middle domains; 1.
PE   3: Inferred from homology;
KW   Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935, ECO:0000256|HAMAP-
KW   Rule:MF_00519};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00519};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00519};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00519};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00519}.
FT   DOMAIN          373..486
FT                   /note="L-arabinose isomerase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11762"
FT   BINDING         317
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT   BINDING         344
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT   BINDING         361
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT   BINDING         460
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
SQ   SEQUENCE   513 AA;  57751 MW;  E92581153BB23A57 CRC64;
     MIKAFENYEI WFITGAQLLY GGDAVKQVDG HSKEMVAGLN DSGRLPIKVV YKGTANSSKE
     VSELFAAANN EKKCIGVITW MHTFSPAKMW IHGLQILHKP LLHLHTQYNA EIPWDSIDMD
     FMNLNQSAHG DREFGHIISR MRIRRKLVVG YWKEEKTQDH IAVWERVCAA WADAQDMLIL
     RFGDQMNNVA VTDGDKVAAE QVLGYHVDYC PFSEVLSYFK EIKDADVDNL VATYFNEYDH
     DSSLEDKTSE AYKKVWNAAK AELALRAILK AKGAKGFTTN FDDLGDVDVE KSGMGFDQIP
     GLASQRLMAE GYGFGAEGDW KSAALYRSIW VMTQGMPNGC SFLEDYTLNF NGEQSSILQS
     HMLEVSPLIA ASKPRLEVHF LGIGVRKSQT ARLVFTSKVG TGVTATVVDL GNRFRMIVND
     VKCIEPKALP KLPVASALWI PQPNFEVGAG CWIYAGGTHH SCFSYDLTEE YWQDYAEIAG
     IECVFINENT KVDEFRKELR FNEVYYMLNK ALL
//
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