ID Q891E3_CLOTE Unreviewed; 479 AA.
AC Q891E3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:AAO36902.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:AAO36902.1};
GN OrderedLocusNames=CTC_02436 {ECO:0000313|EMBL:AAO36902.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36902.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO36902.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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DR EMBL; AE015927; AAO36902.1; -; Genomic_DNA.
DR RefSeq; WP_011100563.1; NC_004557.1.
DR AlphaFoldDB; Q891E3; -.
DR STRING; 212717.CTC_02436; -.
DR GeneID; 24254848; -.
DR KEGG; ctc:CTC_02436; -.
DR HOGENOM; CLU_024775_3_1_9; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR42720:SF1; GLYCEROL 3-PHOSPHATE OXIDASE; 1.
DR PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AAO36902.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT DOMAIN 3..352
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 397..450
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 479 AA; 52794 MW; F503220B9983BE99 CRC64;
MYDVIIIGAG ITGTAIAREL SKYKLNTCVL ERCNDIGMGT SKANSAIVHP GEDPKPGSLK
AKLNVKGNAM YEELSEELDF PFKRIGALVL CFDEKDLDEL KLLKEQGEKN GVPGMEILNR
EETLKLEPNL SEYVVASLHL PSGGIMCPFR ANVAFAENAY TNGVDFKLNT EVKNIVKKED
RYIIETNEGD IEAKIVINAA GVYADVINNM VSENKIKIIP RKGEYCLFDK MVGDTVSKTI
FQLPTKFGKG VLVTPTVDGN LLVGPNAIDI EDKEDVTTDK ESLDYILDKA KMSIKEVPTS
FIITSFSGLR AKGHTGDFII GEVEDAKNFI NVAAIESPGL SSAPAIAEMI GEIIVEKLSP
EKNKQFNPKR EPVKRFEDMN NEEREKAVKE NPLYGNVVCR CEMVTEAEIV DAIKRPLGAR
DLDGIKRRSR AGAGRCQAGF CTPKLVEILS RELEKLPKDV TKFGRESQLI TGGRNKDNI
//
