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Database: UniProt
Entry: A6M0S2_CLOB8
LinkDB: A6M0S2_CLOB8
Original site: A6M0S2_CLOB8 
ID   A6M0S2_CLOB8            Unreviewed;       353 AA.
AC   A6M0S2;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:ABR36202.1};
GN   OrderedLocusNames=Cbei_4092 {ECO:0000313|EMBL:ABR36202.1};
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR36202.1, ECO:0000313|Proteomes:UP000000565};
RN   [1] {ECO:0000313|EMBL:ABR36202.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
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   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR36202.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=21962126; DOI=10.1186/1471-2164-12-479;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Single-nucleotide resolution analysis of the transcriptome structure of
RT   Clostridium beijerinckii NCIMB 8052 using RNA-Seq.";
RL   BMC Genomics 12:479-479(2011).
RN   [3] {ECO:0000313|EMBL:ABR36202.1, ECO:0000313|Proteomes:UP000000565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX   PubMed=22433311; DOI=10.1186/1471-2164-13-102;
RA   Wang Y., Li X., Mao Y., Blaschek H.P.;
RT   "Genome-wide dynamic transcriptional profiling in clostridium beijerinckii
RT   NCIMB 8052 using single-nucleotide resolution RNA-Seq.";
RL   BMC Genomics 13:102-102(2012).
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:PIRSR000112-1};
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DR   EMBL; CP000721; ABR36202.1; -; Genomic_DNA.
DR   RefSeq; WP_012060249.1; NC_009617.1.
DR   AlphaFoldDB; A6M0S2; -.
DR   KEGG; cbe:Cbei_4092; -.
DR   eggNOG; COG0371; Bacteria.
DR   HOGENOM; CLU_038362_0_1_9; -.
DR   Proteomes; UP000000565; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd08174; G1PDH-like; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR032837; G1PDH.
DR   InterPro; IPR016205; Glycerol_DH.
DR   PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43616:SF5; GLYCEROL DEHYDROGENASE 1; 1.
DR   Pfam; PF13685; Fe-ADH_2; 1.
DR   PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000112-1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000112-3};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   BINDING         97..101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         119..122
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         124
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT   BINDING         128
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         171
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         250
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         266
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   353 AA;  39366 MW;  C2538A49DC258973 CRC64;
     MKTSTHRIAI PSILEVGKGN INNVGNLIKK AMFKNVLICF GEGLEELFGE SIRNSLKEAN
     IGISRIETIS DINFEKISVK AFEISNDVEA LIGVGGGKAI DAVKYMSFLR KLPFVSIPTS
     TSNDGFSSAG ASLLVNGRRM SLPAKTPYGI IVDIDVIKSA PEKFIYSGIG DLVSNITALY
     DWKFEEENGR IIIDDFATMI SKKAVNSFIR TEFKNIKDDL FLKELVDSLI LNGISMEIAG
     NSSPASGSEH LISHALDKFL EMPQLHGIQV GIATYIMAKV QDHRFERISK ILKETNFFEH
     AKTLKMKRKD YKNAIDIAPS IKPNRYTYIH VDENRILAKK IIDEDEILNY ILI
//
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