ID   C6WKG1_ACTMD            Unreviewed;       579 AA.
AC   C6WKG1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=Amir_6411 {ECO:0000313|EMBL:ACU40212.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU40212.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU40212.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC   NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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}.
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DR   EMBL; CP001630; ACU40212.1; -; Genomic_DNA.
DR   RefSeq; WP_015805095.1; NC_013093.1.
DR   AlphaFoldDB; C6WKG1; -.
DR   STRING; 446462.Amir_6411; -.
DR   KEGG; ami:Amir_6411; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000002213; 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: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:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 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.
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:UP000002213}.
FT   DOMAIN          33..384
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          409..532
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  62920 MW;  EE717B6F106B5E7B CRC64;
     MATRNPSRTS ATGRLGPEDR ERSWRRLGEE TFDLVIVGGG VVGVGAALDA ATRGLKVALV
     EARDLASGTS SRSSKLFHGG LRYLEQLEFG LVREALRERE LMLTKIAPHL VKPVSFLYPL
     TNRVWERPYT AAGLLMYDTM GGARSVPGQK HLSRSGALRL APSLKQDALI GGIRYFDAQA
     DDARHTMMVG RTAAHYGAVV RPSTQVIDFL HESDRVSGVR VRDVEDGRET DVRAHAVINA
     TGVWTDELQR LSGSRGRFRV RASKGVHIVV PRDRIVSETG LILRTEKSVL FVIPWRNHWI
     IGTTDTDWNL DLSHPAATKA DIDYLLAQVN SVLATPLAHE DIEGVYAGLR PLLAGESEST
     SKLSREHAVA RVAPGLVAIA GGKYTTYRVM GADAVNAASV DLPGRIQPSI TDKVPLVGAD
     GYHALVNQAD HLAAEHGLHP YRVRHLLDRY GSLVHEVLAL AADSPELLKP IPGSPDYLQV
     EVVYAASHEG ALHLEDVLTR RTRISIEYPH RGVESAEAVA GLMAGVLGWD EAAIAREVEV
     YTARVEAERA SQDEPSDQAA DAVRAAAPEV RPELVEPVS
//