ID A0A399CZ95_9BACT Unreviewed; 149 AA.
AC A0A399CZ95;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=RpiB/LacA/LacB family sugar-phosphate isomerase {ECO:0000313|EMBL:RIH63721.1};
GN ORFNames=D1164_18380 {ECO:0000313|EMBL:RIH63721.1};
OS Mariniphaga sediminis.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1628158 {ECO:0000313|EMBL:RIH63721.1, ECO:0000313|Proteomes:UP000266441};
RN [1] {ECO:0000313|EMBL:RIH63721.1, ECO:0000313|Proteomes:UP000266441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY21 {ECO:0000313|EMBL:RIH63721.1,
RC ECO:0000313|Proteomes:UP000266441};
RX PubMed=26012581; DOI=10.1099/ijs.0.000354;
RA Wang F.Q., Shen Q.Y., Chen G.J., Du Z.J.;
RT "Mariniphaga sediminis sp. nov., isolated from coastal sediment.";
RL Int. J. Syst. Evol. Microbiol. 65:2908-2912(2015).
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC {ECO:0000256|ARBA:ARBA00008754}.
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:RIH63721.1}.
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DR EMBL; QWET01000017; RIH63721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399CZ95; -.
DR OrthoDB; 1778624at2; -.
DR Proteomes; UP000266441; Unassembled WGS sequence.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR InterPro; IPR003500; RpiB_LacA_LacB.
DR InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1.
DR PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1.
DR Pfam; PF02502; LacAB_rpiB; 1.
DR PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:RIH63721.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266441}.
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT BINDING 14..15
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 72..76
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 105
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 115
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 138
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT BINDING 142
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ SEQUENCE 149 AA; 16566 MW; 0A9C9279E81CDF7E CRC64;
MKKLDDKTIA LASDHAGFDK KQAIIRFFEE NGILYKDFGC YTNESCDYPD FAHAIADAID
KGEFEIGITF CGSGQGISIT ANKHQNVRSA LCWNPEIGVL AKQHNNANIC AIPSRFVTDE
EAISIVRAYL NAEFEGGRHE RRVAKIPLK
//
