GLD1_SCHPO
ID GLD1_SCHPO Reviewed; 450 AA.
AC O13702;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glycerol dehydrogenase 1;
DE Short=GDH;
DE Short=GLDH;
DE EC=1.1.1.6;
GN Name=gld1; ORFNames=SPAC13F5.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=20396879; DOI=10.1007/s00253-010-2586-3;
RA Matsuzawa T., Ohashi T., Hosomi A., Tanaka N., Tohda H., Takegawa K.;
RT "The gld1+ gene encoding glycerol dehydrogenase is required for glycerol
RT metabolism in Schizosaccharomyces pombe.";
RL Appl. Microbiol. Biotechnol. 87:715-727(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE,
RP AND COFACTOR.
RA Mulichak A.M.;
RT "Crystal structure of glycerol dehydrogenase from Schizosaccharomyces
RT pombe.";
RL Submitted (AUG-2005) to the PDB data bank.
CC -!- FUNCTION: Glycerol dehydrogenase involved in the assimilation of
CC glycerol. {ECO:0000269|PubMed:20396879}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH;
CC Xref=Rhea:RHEA:13769, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.6;
CC Evidence={ECO:0000269|PubMed:20396879};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|Ref.4};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|Ref.4};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Repressed by glucose. {ECO:0000269|PubMed:20396879}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11766.1; -; Genomic_DNA.
DR PIR; T37628; T37628.
DR RefSeq; NP_593651.1; NM_001019083.2.
DR PDB; 1TA9; X-ray; 1.90 A; A/B=1-450.
DR PDBsum; 1TA9; -.
DR AlphaFoldDB; O13702; -.
DR SMR; O13702; -.
DR BioGRID; 279326; 71.
DR STRING; 4896.SPAC13F5.03c.1; -.
DR iPTMnet; O13702; -.
DR MaxQB; O13702; -.
DR PaxDb; O13702; -.
DR EnsemblFungi; SPAC13F5.03c.1; SPAC13F5.03c.1:pep; SPAC13F5.03c.
DR GeneID; 2542881; -.
DR KEGG; spo:SPAC13F5.03c; -.
DR PomBase; SPAC13F5.03c; gld1.
DR VEuPathDB; FungiDB:SPAC13F5.03c; -.
DR eggNOG; ENOG502QUB4; Eukaryota.
DR HOGENOM; CLU_044754_1_0_1; -.
DR InParanoid; O13702; -.
DR OMA; IHNMPFP; -.
DR PhylomeDB; O13702; -.
DR BRENDA; 1.1.1.6; 5613.
DR UniPathway; UPA00617; UER00668.
DR EvolutionaryTrace; O13702; -.
DR PRO; PR:O13702; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IMP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISS:PomBase.
DR GO; GO:0019564; P:aerobic glycerol catabolic process; IMP:PomBase.
DR GO; GO:0042149; P:cellular response to glucose starvation; IC:GOC-OWL.
DR GO; GO:0061613; P:glycolytic process from glycerol; IMP:PomBase.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; PTHR43616; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycerol metabolism; Metal-binding; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..450
FT /note="Glycerol dehydrogenase 1"
FT /id="PRO_0000314770"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 155..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 177..180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.4"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:1TA9"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 223..245
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 258..284
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 289..307
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 333..347
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 352..364
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:1TA9"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1TA9"
FT HELIX 407..428
FT /evidence="ECO:0007829|PDB:1TA9"
SQ SEQUENCE 450 AA; 49433 MW; E25248204A92E33A CRC64;
MIGPRLCAAT PRFPLVSLAH RNSKVFALAS SNAVAQRWGK RFYAPIETET PHKVGVEFEE
SKDRIFTSPQ KYVQGRHAFT RSYMYVKKWA TKSAVVLADQ NVWNICANKI VDSLSQNGMT
VTKLVFGGEA SLVELDKLRK QCPDDTQVII GVGGGKTMDS AKYIAHSMNL PSIICPTTAS
SDAATSSLSV IYTPDGQFQK YSFYPLNPNL IFIDTDVIVR APVRFLISGI GDALSTWVET
ESVIRSNSTS FAGGVASIAG RYIARACKDT LEKYALSAIL SNTRGVCTEA FENVVEANTL
MSGLGFENGG LAAAHAIHNG MTAIHGPVHR LMHGEKVAYG TLVQVVLEDW PLEDFNNLAS
FMAKCHLPIT LEELGIPNVT DEELLMVGRA TLRPDESIHN MSKKFNPSQI ADAIKAVDSY
SQKWQEQTGW TERFRLPPSR HSPHLTDIHP
