(data stored in SCRATCH zone)

SWISSPROT: A5GRE5_SYNR3

ID   A5GRE5_SYNR3            Unreviewed;       378 AA.
AC   A5GRE5;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   SubName: Full=Glycerol dehydrogenase {ECO:0000313|EMBL:CAK27454.1};
DE            EC=1.1.1.6 {ECO:0000313|EMBL:CAK27454.1};
GN   Name=gldH {ECO:0000313|EMBL:CAK27454.1};
GN   OrderedLocusNames=SynRCC307_0551 {ECO:0000313|EMBL:CAK27454.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27454.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-
CC       1};
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DR   EMBL; CT978603; CAK27454.1; -; Genomic_DNA.
DR   RefSeq; WP_011934969.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0551; -.
DR   EnsemblBacteria; CAK27454; CAK27454; SynRCC307_0551.
DR   KEGG; syr:SynRCC307_0551; -.
DR   eggNOG; ENOG4105DCT; Bacteria.
DR   eggNOG; COG0371; LUCA.
DR   HOGENOM; HOG000031784; -.
DR   KO; K00005; -.
DR   OMA; ETMHNEP; -.
DR   OrthoDB; 717704at2; -.
DR   BioCyc; SSP316278:G1GJL-538-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR016205; Glycerol_DH.
DR   PANTHER; PTHR43616; PTHR43616; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
PE   4: Predicted;
DR   PRODOM; A5GRE5.
DR   SWISS-2DPAGE; A5GRE5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000112-1};
KW   NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW   Oxidoreductase {ECO:0000313|EMBL:CAK27454.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   DOMAIN       21    361       Fe-ADH. {ECO:0000259|Pfam:PF00465}.
FT   NP_BIND     109    113       NAD. {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   NP_BIND     131    134       NAD. {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   METAL       186    186       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR000112-1}.
FT   METAL       269    269       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR000112-1}.
FT   METAL       286    286       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR000112-1}.
FT   BINDING     136    136       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000112-2}.
FT   BINDING     140    140       NAD. {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   BINDING     142    142       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   BINDING     146    146       NAD. {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   BINDING     186    186       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000112-2}.
FT   BINDING     269    269       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000112-2}.
FT   BINDING     286    286       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000112-2}.
SQ   SEQUENCE   378 AA;  39754 MW;  EDA66C85152EC62F CRC64;
     MAYRTDFGSI HQRPLGVFGA PARYVQGPGA TWELGRELQR LGFQGPVLFI AGGTAQRTLA
     PIWQEQLPPV GLQPVIDAFG GECSESEIKR LVGMSDHHGF CAVVGAGGGK ASDTARAVAD
     ELGLPVVITP TLASTDSPCS ALSVIYSDEG SVTGFRFYNR HPELLLVDTE VIAKAPKRQL
     VAGLGDGLAT WFEARATHES HRNNVVGGKP LTSALMLAKL CHDILLADGP AACAAIDAGV
     PTPALERIVE ANILLSGLGF EIGGLALAHA VHNGISTIPG SHHNLHGEKV VIGLHTQLVL
     EGQPQSEIDA VFRYCQQVGL PTTLAQVGID ASNDAELMAI AERSVIPGET SHNEPFEVTA
     IAVMRALKAA DQLGRAYL
//

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