DDGAH_PSEA6
ID DDGAH_PSEA6 Reviewed; 341 AA.
AC Q15SS1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase {ECO:0000305};
DE EC=1.1.1.389 {ECO:0000269|Ref.2};
DE AltName: Full=2-keto-3-deoxy-L-galactonate 5-dehydrogenase {ECO:0000303|Ref.2};
GN OrderedLocusNames=Patl_2551 {ECO:0000312|EMBL:ABG41067.1};
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=T6c / ATCC BAA-1087;
RX DOI=10.1007/s12257-014-0622-3;
RA Lee S.B., Cho S.J., Kim J.A., Lee S.Y., Kim S.M., Lim H.S.;
RT "Metabolic pathway of 3,6-anhydro-L-galactose in agar-degrading
RT microorganisms.";
RL Biotechnol. Bioprocess Eng. 19:866-878(2014).
CC -!- FUNCTION: Involved in the degradation of 3,6-anhydro-L-galactose, which
CC is the major monomeric sugar of red macroalgae. Catalyzes the third
CC step of the pathway, the NAD(+)-dependent oxidation of 2-dehydro-3-
CC deoxy-L-galactonate (L-KDGal) to 3-deoxy-D-glycero-2,5-hexodiulosonate
CC (L-DDGal). {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-L-galactonate + NAD(+) = 3-deoxy-D-glycero-
CC 2,5-hexodiulosonate + H(+) + NADH; Xref=Rhea:RHEA:47988,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29071, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:75545; EC=1.1.1.389;
CC Evidence={ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O58389};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O58389};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CP000388; ABG41067.1; -; Genomic_DNA.
DR RefSeq; WP_011575333.1; NC_008228.1.
DR AlphaFoldDB; Q15SS1; -.
DR SMR; Q15SS1; -.
DR STRING; 342610.Patl_2551; -.
DR DNASU; 4174306; -.
DR EnsemblBacteria; ABG41067; ABG41067; Patl_2551.
DR KEGG; pat:Patl_2551; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_6; -.
DR OMA; FWKAGRI; -.
DR OrthoDB; 972769at2; -.
DR BioCyc; MetaCyc:MON-19466; -.
DR Proteomes; UP000001981; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..341
FT /note="2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase"
FT /id="PRO_0000449954"
FT ACT_SITE 39
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT ACT_SITE 42
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT SITE 145
FT /note="Important for catalytic activity for the proton
FT relay mechanism but does not participate directly in the
FT coordination of zinc atom"
FT /evidence="ECO:0000250|UniProtKB:O58389"
SQ SEQUENCE 341 AA; 36373 MW; DA7953D0BD64C4F0 CRC64;
MFAAQYIGNK SFNVVEGHAI APQAGEVRLD VGYVGICGTD MHIYHGVMDQ RVSIPQTIGH
EISGVVAQIG EGVEGFTVGE KVVVRPLDWC GECPTCEAGL THICQNLKFM GIDTPGAFQS
SWTVKARTLH KLPAGVDLKQ GALVEPLSVA CHDVRRSRLK AGEKAVILGG GPIGQLVAAV
AKSVGAEVLV SEPNDSRREF ADELGVKSVN PMDTDLAAYV DQWTGTKGAD VVFEVSGVLP
AIQSMTQIAG RRGRIVMVAI HSTAPPIDLF QFFWKELELL GARVYEAADF DWAIELIASG
QIDLKPFISS VSPLADIGSA FANMDGNPQG MKALVECNAE Q
