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Database: UniProt
Entry: E4HGN7_9ACTN
LinkDB: E4HGN7_9ACTN
Original site: E4HGN7_9ACTN 
ID   E4HGN7_9ACTN            Unreviewed;       392 AA.
AC   E4HGN7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:EFS93595.1};
GN   ORFNames=HMPREF9607_00049 {ECO:0000313|EMBL:EFS93595.1};
OS   Cutibacterium modestum HL044PA1.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium; Cutibacterium modestum.
OX   NCBI_TaxID=765109 {ECO:0000313|EMBL:EFS93595.1, ECO:0000313|Proteomes:UP000003179};
RN   [1] {ECO:0000313|EMBL:EFS93595.1, ECO:0000313|Proteomes:UP000003179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL044PA1 {ECO:0000313|EMBL:EFS93595.1,
RC   ECO:0000313|Proteomes:UP000003179};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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:EFS93595.1}.
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DR   EMBL; ADZU01000003; EFS93595.1; -; Genomic_DNA.
DR   RefSeq; WP_002526976.1; NZ_GL383170.1.
DR   AlphaFoldDB; E4HGN7; -.
DR   GeneID; 73017520; -.
DR   PATRIC; fig|765109.3.peg.45; -.
DR   HOGENOM; CLU_038362_1_0_11; -.
DR   Proteomes; UP000003179; 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; cd08175; G1PDH; 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   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   NAD {ECO:0000256|ARBA:ARBA00023027}; 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}.
SQ   SEQUENCE   392 AA;  41394 MW;  1E290516F5CC6FAA CRC64;
     MRDTIIEAAL TSARDTDTVV IGRGAVARTG KAIRDAMDTS TDCEMRPAMI VADDCTWHVA
     GNKVTAALAE ARIPVVEPLV FPATPTLYAS LDNANRIAKV LRDRDFQRGV TVIPVAVGSG
     TINDLTKLAA RDLGRRYAVV GTAASMDGYT GAGAPISDNG VKITMNCVAP QVVVFDLDLA
     ANAPSPMSAS GFGDLSAKIP GGADWLIADA AGVESIDEDV WTLVQSGVHE ALSRPADLAA
     GVPEAYEGLV KGLILSGLAM QVYDGTRPAS GAEHYFSHIW ELAHVGAKLD PPLSHGFKVA
     IGTLAMLTFY EKFLDRDPAT IDIDAAVAKW PTWDVVEADI RHTFDGALAD HAVKETRVKF
     VDRDWPPWAA GPLCVEMAGN SRPSSGTASA CR
//
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