ID D1PI57_9FIRM Unreviewed; 492 AA.
AC D1PI57;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 68.
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 ECO:0000313|EMBL:EFB77612.1};
GN ORFNames=SUBVAR_04022 {ECO:0000313|EMBL:EFB77612.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB77612.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB77612.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB77612.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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:EFB77612.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACBY02000004; EFB77612.1; -; Genomic_DNA.
DR RefSeq; WP_007045469.1; NZ_GG704769.1.
DR AlphaFoldDB; D1PI57; -.
DR STRING; 411471.SUBVAR_04022; -.
DR GeneID; 78307408; -.
DR eggNOG; COG2160; Bacteria.
DR HOGENOM; CLU_045663_0_0_9; -.
DR OrthoDB; 9765600at2; -.
DR UniPathway; UPA00145; UER00565.
DR Proteomes; UP000003438; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003438}.
FT DOMAIN 355..469
FT /note="L-arabinose isomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11762"
FT BINDING 299
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 326
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 343
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
FT BINDING 443
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00519"
SQ SEQUENCE 492 AA; 55145 MW; 6CC31E06C3EF3EB8 CRC64;
MHMQDYEFWF VVGSQFLYGP EVLETVAKRA AEMTEVLNAS GNLPCKIVYK VTAKTNKEIA
DVVREANYDP RCAGIITWCH TFSPSKMWIN GFVDLQKPYC HFATQYNREI PNEEIDMDFM
NLNQAAHGDR EHGFIAARLR MPRKIIAGYW QDEEVQKRLG RWMRVAVGVA VSRDLKVMRF
GDNMREVAVT EGDKVEVQAK LGWQVNTWAV GDLVKVMHEV TDAEIDALME VYRASYEIAT
DDIDAIRYQA REEIAIKKML DAEGCKAFSN TFQDLYGMEQ LPGLASQHLM AQGYGYGGEG
DWKVAAMTAI LKAMGEGGNG CSLFMEDYTY NLVPGAEYSL GAHMLEVCPC CAAEKPRIET
HPLGIGMNEK DPARLVFEGK PGKAIVVSLI DMGGRLRLIC QDIECVKPIL PMPNLPVARV
MWKALPSLTT GVECWITAGG AHHTVLSYDV TAEQMHDWAN IMGIEFVHIG KDTTPEGLEH
DLFLADLAWK LK
//
