ID M1PCQ2_DESSD Unreviewed; 525 AA.
AC M1PCQ2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:AGF77505.1};
GN OrderedLocusNames=UWK_00931 {ECO:0000313|EMBL:AGF77505.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF77505.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR EMBL; CP003985; AGF77505.1; -; Genomic_DNA.
DR RefSeq; WP_015403201.1; NC_020304.1.
DR AlphaFoldDB; M1PCQ2; -.
DR STRING; 1167006.UWK_00931; -.
DR KEGG; dsf:UWK_00931; -.
DR PATRIC; fig|1167006.5.peg.1043; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_4_1_7; -.
DR OMA; GVMTIMN; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000011721; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap 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; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT DOMAIN 19..378
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 417..505
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 525 AA; 58295 MW; 919767CBF3EC7292 CRC64;
MKRERMLVNI RKQGSKPWDI IVIGGGATGL GTALDAASRG YHTLLLEQDD FSKGTSSRST
KLVHGGVRYL AQGDVSLVLE ALHERGLMRH NAPHLVKNQS FIIPNYDWWD GPFYTVGMKV
YDMMAGKLGL GPSQSLSSDE VLRAIPNLKT EGLRGGVIYY DGQFDDSRLA INIAQTCAEH
GGVLLNYMRV SGLTKSGDGI ISGVEAVDLE SGETYSLLSK SVVNATGVFV DEIMKMDDPD
ALPLVRPSQG VHIILDKQFL KGESAIMIPK TSDGRVLFAV PWHDRVVVGT TDTPLDECSL
EPRALEEEIE FILSTAKKYL TREPQRKDIL SIFAGLRPLA APEEGSDGSS TKEISRSHHL
RVSLSGLVTI TGGKWTTYRK MAEDTVDKAA LVGGLKQQKC RTEDMPIHGW LANVDYHDPL
YYYGSDADYM RDLVMDHPEL GEQLHPGLPY TPIEVIWSAR YEMARTVEDI LARRQRALFL
DARAAIEMAP AVAKILAKEL GRDKEWQELQ VREFTELARG YYLLD
//