ID W1X2C0_ECOLX Unreviewed; 500 AA.
AC W1X2C0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=Q609_ECAC01382G0004 {ECO:0000313|EMBL:ETJ24612.1};
OS Escherichia coli DORA_A_5_14_21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1403943 {ECO:0000313|EMBL:ETJ24612.1, ECO:0000313|Proteomes:UP000018853};
RN [1] {ECO:0000313|EMBL:ETJ24612.1, ECO:0000313|Proteomes:UP000018853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DORA_A_5_14_21 {ECO:0000313|Proteomes:UP000018853};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) 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 -!- SUBUNIT: Homohexamer. {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:ETJ24612.1}.
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DR EMBL; AZLZ01001382; ETJ24612.1; -; Genomic_DNA.
DR AlphaFoldDB; W1X2C0; -.
DR PATRIC; fig|1403943.3.peg.1753; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000018853; 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 CDD; cd03557; L-arabinose_isomerase; 1.
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 363..476
FT /note="L-arabinose isomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11762"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 450
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
SQ SEQUENCE 500 AA; 56074 MW; 605FB5AC9FAA0FB2 CRC64;
MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT KAKLPCKLVL KPLGTTPDEI
TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF
MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR
FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT
PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG
YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAA
EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP
KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT
RLPAFKDALR WNEVYYGFRR
//
