PLH5_FORAG
ID PLH5_FORAG Reviewed; 280 AA.
AC T2KN98;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
DE EC=5.3.1.17 {ECO:0000255|HAMAP-Rule:MF_00687};
DE AltName: Full=5-keto-4-deoxyuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
DE AltName: Full=DKI isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
DE AltName: Full=P5_isomerase {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P5 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P5;
GN Name=kduI {ECO:0000255|HAMAP-Rule:MF_00687}; ORFNames=BN863_21940;
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX PubMed=23995932; DOI=10.1128/aem.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA Bornscheuer U.T., Hehemann J.H.;
RT "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT ulvan.";
RL Nat. Chem. Biol. 15:803-812(2019).
CC -!- FUNCTION: Isomerase involved in ulvan degradation (Probable). Ulvan is
CC the main polysaccharide component of the Ulvales (green seaweed) cell
CC wall. It is composed of disaccharide building blocks comprising 3-
CC sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-
CC iduronic acid (IduA), or D-xylose (Xyl) (Probable). Catalyzes the
CC isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-
CC 2,5-hexodiulosonate (By similarity). {ECO:0000255|HAMAP-Rule:MF_00687,
CC ECO:0000305|PubMed:31285597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-
CC hexodiulosonate; Xref=Rhea:RHEA:23896, ChEBI:CHEBI:17117,
CC ChEBI:CHEBI:29071; EC=5.3.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00687};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00687};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00687};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- SIMILARITY: Belongs to the KduI family. {ECO:0000255|HAMAP-
CC Rule:MF_00687}.
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DR EMBL; HG315671; CDF79906.1; -; Genomic_DNA.
DR RefSeq; WP_038530484.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KN98; -.
DR SMR; T2KN98; -.
DR STRING; 1347342.BN863_21940; -.
DR EnsemblBacteria; CDF79906; CDF79906; BN863_21940.
DR PATRIC; fig|1347342.6.peg.2201; -.
DR eggNOG; COG3717; Bacteria.
DR HOGENOM; CLU_062609_0_0_10; -.
DR OMA; TFIWAMA; -.
DR OrthoDB; 1047507at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008697; F:4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 2.60.120.520; -; 1.
DR HAMAP; MF_00687; KduI; 1.
DR InterPro; IPR007045; KduI.
DR InterPro; IPR021120; KduI/IolB_isomerase.
DR InterPro; IPR027449; KduI_N.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR38461; PTHR38461; 1.
DR Pfam; PF04962; KduI; 1.
DR PIRSF; PIRSF006625; KduI; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..280
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT isomerase"
FT /id="PRO_0000448314"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
SQ SEQUENCE 280 AA; 31396 MW; 5DE3CAD0AAD8A085 CRC64;
MSTKYESRYA SSPQTVKQYD TQELRNEFLI DNLMQNDTIN LTYTHYDRYI AGSAVPTSSP
LTLETIDPLK SEYFLERREL GIINVGGTGS VTVDGTVYEL GLKDALYVGM GNKDVVFASD
DASNPAQFYL NSAPAHTNYP TKKVSKAEAN KIELGTLETA NHRTVNQMII GGIVTTCQLQ
MGMTELKTGS VWNTMPAHVH NRRMEVYLYI DIPQDQAVCH FMGEPQETRH IWMQNNQAVI
SPPWSIHSGS GTSNYTFVWG MAGENLDYND MDVAKITELR
