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Database: UniProt
Entry: R5YSX3_9FIRM
LinkDB: R5YSX3_9FIRM
Original site: R5YSX3_9FIRM 
ID   R5YSX3_9FIRM            Unreviewed;       351 AA.
AC   R5YSX3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:CDA24531.1};
GN   ORFNames=BN528_01385 {ECO:0000313|EMBL:CDA24531.1};
OS   Roseburia sp. CAG:197.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=1262943 {ECO:0000313|EMBL:CDA24531.1, ECO:0000313|Proteomes:UP000018336};
RN   [1] {ECO:0000313|EMBL:CDA24531.1, ECO:0000313|Proteomes:UP000018336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:197 {ECO:0000313|Proteomes:UP000018336};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:PIRSR000112-1};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA24531.1}.
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DR   EMBL; CBBL010000095; CDA24531.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5YSX3; -.
DR   Proteomes; UP000018336; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000018336};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   BINDING         95..99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         117..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         122
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT   BINDING         126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT   BINDING         169
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         248
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT   BINDING         264
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ   SEQUENCE   351 AA;  38790 MW;  C9C241B477ED5208 CRC64;
     MGDNHIAIPA LLKIGPGALG ELGTYLKDLR LEKVVILFGN GLIEMFGMDV MKSLAEMGID
     VLEYQELDTV RLEDLTSLAF SMPAKTQAVI GIGGGKVIDA AKYCGFLRNL AFISIPTSAS
     SDGFSSASAS LLVEGRRKSV PARLAYGIVV DTQIIKSAPK KFIYSGIGDM VSKITALYDW
     KFEEEHGYGK VNDFATMIAK KAVNSFVRTP FESIEEDLFI KELLDSLAMS GIANEIAGSS
     APTSGSEHLI SHALDKMLEQ PQLHGIQVGI ATYLMSVVQD HRYKRVNTIF TQTGFWDFVK
     TLEMRHVDFE QAIDLAPSIK PFRHTYLHEQ EYRDRAKEVL ATDEKLKEIL V
//
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