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Database: UniProt
Entry: A0A2C9SZK4_9MYCO
LinkDB: A0A2C9SZK4_9MYCO
Original site: A0A2C9SZK4_9MYCO 
ID   A0A2C9SZK4_9MYCO        Unreviewed;       511 AA.
AC   A0A2C9SZK4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   Name=glpD1 {ECO:0000313|EMBL:GAY17004.1};
GN   ORFNames=MSZK_37300 {ECO:0000313|EMBL:GAY17004.1};
OS   Mycobacterium sp. shizuoka-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=2039281 {ECO:0000313|EMBL:GAY17004.1, ECO:0000313|Proteomes:UP000223528};
RN   [1] {ECO:0000313|EMBL:GAY17004.1, ECO:0000313|Proteomes:UP000223528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=shizuoka-1 {ECO:0000313|Proteomes:UP000223528};
RA   Yoshida M., Izumiyama S., Fukano H., Sugiyama K., Suzuki M., Shibayama K.,
RA   Hoshino Y.;
RT   "Draft genome sequence of Mycobacterium sp. shizuoka-1.";
RL   Submitted (OCT-2017) 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   -!- 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:GAY17004.1}.
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DR   EMBL; BEWG01000064; GAY17004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9SZK4; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000223528; Unassembled WGS sequence.
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:UP000223528}.
FT   DOMAIN          26..352
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   511 AA;  53548 MW;  D1E8CFE5C266F386 CRC64;
     MSDLTALNAA RRTTDLADLG DDGRVDVVVI GGGITGTGIA LDAASRGLSV LLVEKHDLAF
     GTSRWSSKLV HGGLRYLATG NVGIARRSAV ERGILMTRNA PHLVHAMAQL VPLLPSMSRA
     QRALVRTGFV AGDALRILAG TKASTLPRSR RIGVPQAVAM APTVRREGLD GGLLAYDGQL
     IDDARLVVAV ARTAAQHGAR ILTRVSAQSA TGTSVRLLDE LTGETLDVAA RVVINATGVW
     AGAVDPAIKL RPSRGTHLVF DAASFGNPTA ALTIPIPGEV NRFVFAMPEQ LGRVYLGLTD
     EDAPGPIPDV PEPTSAETSF LLDTVNTALG TALGRGDIRG AYAGLRPLID TGTGRTSDLS
     REHAVIESES GVFSIVGGKL TEYRHMAQDA LDRALAARAI TAQPCRTRNL PLVGAPANPV
     ATLRTTSELP GSLVARYGAE SPNVIASARC DRPTDPVADG IDVTRAEFEF AVTHEGALTA
     DDIVDRRTRI GLVETDRDRV LAVAGDLLAR A
//
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