ID   G8RLV3_MYCRN            Unreviewed;       509 AA.
AC   G8RLV3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=MycrhN_4432 {ECO:0000313|EMBL:AEV74926.1};
OS   Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV74926.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV74926.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV74926.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003169; AEV74926.1; -; Genomic_DNA.
DR   RefSeq; WP_014212674.1; NC_016604.1.
DR   AlphaFoldDB; G8RLV3; -.
DR   STRING; 710685.MycrhN_4432; -.
DR   KEGG; mrh:MycrhN_4432; -.
DR   PATRIC; fig|710685.3.peg.4443; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000005442; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 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; PS00977; FAD_G3PDH_1; 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   ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT   DOMAIN          26..351
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          405..498
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   509 AA;  53328 MW;  76B1625D4E048F22 CRC64;
     MTSSTALNEA RRAAELTALA DGDTIDVVVI GGGITGVGIA LDAVTRGLSV ALVEKHDLAF
     GTSRWSSKLV HGGLRYLASG NVGIARRSAV ERGILMTRNA PHLVSAMPQL VPLLPSMNAA
     SRALVRFGFA AGDGLRKLAG TPSSTLPRSR RIDARRAVEL APTVRRDGLA GALLAYDGQL
     IDDARLVTAV ARTAAQHGAV ILTHVAASNA TGTSVTLTDQ RSGESFDVSA RAVINATGVW
     AGEVDASVRL RPSRGTHLVF DAASFGNPVA ALTIPIPGEI NRFVFAMPEQ LGRVYLGLTD
     EDAPGPIPDV PQPTPEETTF LLDTVNTALD VALQPDDVIG AYAGLRPLID AGGGRTADVS
     REHRVDESPS GLISVIGGKL TEYRFMAEDV LDRAVALRGL SAAGCRTRNL PLVGAPSNSV
     ATLRSPIELP SSLVSRYGAE APNVIAAASC DRPTDQVADG IDVIRAEFEY AVTHEGALTV
     DDIVDRRTRI GLVSADRDRV VDVAKEFVV
//