AHGD_VIBSJ
ID AHGD_VIBSJ Reviewed; 480 AA.
AC H2IFE7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=3,6-anhydro-alpha-L-galactose dehydrogenase {ECO:0000305};
DE Short=AHG dehydrogenase {ECO:0000303|PubMed:25156229};
DE EC=1.2.1.92 {ECO:0000269|PubMed:25156229};
GN Name=Vejahgd {ECO:0000303|PubMed:25156229};
GN ORFNames=VEJY3_09240 {ECO:0000312|EMBL:AEX22330.1};
OS Vibrio sp. (strain EJY3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1116375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EJY3;
RX PubMed=22535948; DOI=10.1128/jb.00303-12;
RA Roh H., Yun E.J., Lee S., Ko H.J., Kim S., Kim B.Y., Song H., Lim K.I.,
RA Kim K.H., Choi I.G.;
RT "Genome sequence of Vibrio sp. strain EJY3, an agarolytic marine bacterium
RT metabolizing 3,6-anhydro-L-galactose as a sole carbon source.";
RL J. Bacteriol. 194:2773-2774(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=EJY3;
RX PubMed=25156229; DOI=10.1111/1462-2920.12607;
RA Yun E.J., Lee S., Kim H.T., Pelton J.G., Kim S., Ko H.J., Choi I.G.,
RA Kim K.H.;
RT "The novel catabolic pathway of 3,6-anhydro-L-galactose, the main component
RT of red macroalgae, in a marine bacterium.";
RL Environ. Microbiol. 17:1677-1688(2015).
CC -!- FUNCTION: Involved in the degradation of 3,6-anhydro-L-galactose, which
CC is the major monomeric sugar of red macroalgae. Catalyzes the oxidation
CC of 3,6-anhydro-L-galactose (AHG) to form 3,6-anhydrogalactonate (AHGA).
CC {ECO:0000269|PubMed:25156229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,6-anhydro-alpha-L-galactopyranose + H2O + NADP(+) = 3,6-
CC anhydro-L-galactonate + 2 H(+) + NADPH; Xref=Rhea:RHEA:40803,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83433, ChEBI:CHEBI:83435; EC=1.2.1.92;
CC Evidence={ECO:0000269|PubMed:25156229};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,6-anhydro-alpha-L-galactopyranose + H2O + NAD(+) = 3,6-
CC anhydro-L-galactonate + 2 H(+) + NADH; Xref=Rhea:RHEA:43568,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:83433, ChEBI:CHEBI:83435; EC=1.2.1.92;
CC Evidence={ECO:0000269|PubMed:25156229};
CC -!- BIOTECHNOLOGY: Could be used for bioconversion of red macroalgal
CC biomass into biofuels or industrial chemicals.
CC {ECO:0000305|PubMed:25156229}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP003241; AEX22330.1; -; Genomic_DNA.
DR RefSeq; WP_014232205.1; NC_016613.1.
DR AlphaFoldDB; H2IFE7; -.
DR SMR; H2IFE7; -.
DR KEGG; vej:VEJY3_09240; -.
DR PATRIC; fig|1116375.3.peg.1847; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_6; -.
DR BioCyc; MetaCyc:MON-18902; -.
DR BRENDA; 1.2.1.92; 6640.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase.
FT CHAIN 1..480
FT /note="3,6-anhydro-alpha-L-galactose dehydrogenase"
FT /id="PRO_0000432212"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT ACT_SITE 282
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 149..150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 173..176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 226..227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 249
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 383
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P25526"
SQ SEQUENCE 480 AA; 53296 MW; 20FD52BF6D48E1F4 CRC64;
MKRYQMYVDG QWIDAENGKV DQVINPSTEE VLAEIQDGDQ DDAERVLSVA KRAQSDWKRV
PARQRAELLR KFAQEIRNNR EHLAELLVSE QGKLYRVALG EVDVAASFIE YACDWARQMD
GDIVQSDNVN EHIWIQKIPR GVVVAITAWN FPFALAGRKI GPALVAGNTI VVKPTSETPL
ATLELGYIAE KVGIPAGVLN IVTGGGASLG GALTSHRYTN MVTMTGSTPV GQQIIKASAN
NMAHVQLELG GKAPFIVMED ADLEQAAAAA LHSRFDNCGQ VCTCNERMYV HSSVYDEFMA
IFMEKVQNIK VGNPMDPESD MGPKVNKREL DHMEALVAQA LKEGAQLLHG GKRLTEGEFG
KGFWFEPTIL GNVQQSMTIV HEEAFGPILP VIKFDTFEEV IDYANDSEYG LATMICTRNM
KYVHRLTHEL ECGEIYVNRG HGEQHQGFHN GYKLSGTGGE DGKYGFEQYL EKKTFYVNFD
