GAL_PSEFL
ID GAL_PSEFL Reviewed; 304 AA.
AC P11886;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Galactose 1-dehydrogenase;
DE EC=1.1.1.48;
GN Name=gal;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-40.
RC STRAIN=BMTU 102;
RX PubMed=2503815; DOI=10.1093/nar/17.13.5402;
RA Sperka S., Zehelein E., Fiedler S., Fischer S., Sommer R., Buckel P.;
RT "Complete nucleotide sequence of Pseudomonas fluorescens D-galactose
RT dehydrogenase gene.";
RL Nucleic Acids Res. 17:5402-5402(1989).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=4153311; DOI=10.1111/j.1432-1033.1974.tb03687.x;
RA Blachnitzky E.O., Wengenmayer F., Kurz G.;
RT "D-Galactose dehydrogenase from Pseudomonas fluorescens. Purification,
RT properties and structure.";
RL Eur. J. Biochem. 47:235-250(1974).
CC -!- FUNCTION: Catalyzes the dehydrogenation of D-galactose by either NAD(+)
CC or NADP(+). Oxidizes following sugars in decreasing order: D-fucose >
CC D-galactose > L-arabinose > 2-deoxy-D-galactose >> 4-deoxy-D-galactose
CC > 2-deoxy-2-amino-D-galactose. {ECO:0000269|PubMed:4153311}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH;
CC Xref=Rhea:RHEA:21296, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15895, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.48;
CC Evidence={ECO:0000269|PubMed:4153311};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for NAD(+) {ECO:0000269|PubMed:4153311};
CC KM=2.3 mM for NADP(+) {ECO:0000269|PubMed:4153311};
CC KM=0.7 mM for D-galactose {ECO:0000269|PubMed:4153311};
CC pH dependence:
CC Optimum pH is between 9.1 and 9.5. {ECO:0000269|PubMed:4153311};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:4153311}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; X14913; CAA33038.1; -; Genomic_DNA.
DR PIR; S04853; S04853.
DR AlphaFoldDB; P11886; -.
DR SMR; P11886; -.
DR KEGG; ag:CAA33038; -.
DR BioCyc; MetaCyc:MON-12890; -.
DR UniPathway; UPA00214; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019151; F:galactose 1-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Galactose metabolism; NAD; Oxidoreductase.
FT CHAIN 1..304
FT /note="Galactose 1-dehydrogenase"
FT /id="PRO_0000087428"
SQ SEQUENCE 304 AA; 33050 MW; D842A776DC67A3B0 CRC64;
MQPIRLGLVG YGKIAQDQHV PAINANPAFT LVSVATQGKP CPGVENFQSL GELLENGPPV
DAIAFCTPPQ GRFALVQQAL AAGKHVLVEK PPCATLGKAA LWIKREQASA PCSPCIAYAP
AIAAARDWLA TRTLQSVQID WKEDVRKWHP GQAWIWQPGL GVFDPGINAL SIVTHLLPLP
LFVESAELRV PSNCQSPIAA SIKMSDPRLL DVRAEFDFDH GHDELWSIQI RCAEGTLRLD
NGGALLSIDG VRQTVAEEGE YAAVYRHFQQ LIGDKTSDVD VQPLRLVADS FFVGSRVSVE
AFYD