ID A0A402ALC6_9CHLR Unreviewed; 559 AA.
AC A0A402ALC6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpA {ECO:0000313|EMBL:GCE19998.1};
GN ORFNames=KDK_37980 {ECO:0000313|EMBL:GCE19998.1};
OS Dictyobacter kobayashii.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=2014872 {ECO:0000313|EMBL:GCE19998.1, ECO:0000313|Proteomes:UP000287188};
RN [1] {ECO:0000313|Proteomes:UP000287188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno11 {ECO:0000313|Proteomes:UP000287188};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) 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:GCE19998.1}.
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DR EMBL; BIFS01000001; GCE19998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402ALC6; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000287188; 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:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000287188}.
FT DOMAIN 22..393
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 416..538
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 559 AA; 61651 MW; E95D3D0C7FA8B148 CRC64;
MQPLSSRERA YNFNELANNS FDILVIGGGI TGAGVALDAV SRGYSVALVE KADFASGTSS
KSTKLVHGGI RYLPNFDIAL VHEALVERGL LLQNAPFLVN PVAFVLPIYE GDKHPVGMPF
TTPKGIGLNR LLDAGLWMYD GLAGRRNISR HHHISRQEVL ERAPTLISEG LKEGFIYYDG
QTNDVRLTMT VLRTAARSGA VIANYAEVTG FEMSHDHITG AVVHDNIGDQ QFTVRARHVV
NATGVFSEQV ESLTGHTPEI QVEPSKGVHL VLSREQLQLG DDAIVLPETE DKRILFIVPW
ESRAIYGTTD TGTGDLNHPN ASQDDITYLL KYLNRYLSVN VTEDDIISTY AGYRPLVKPR
QKNASTAKLS RTHAVIESPS GLVTITGGKL TTYRRMAQDT LDLISRRDSM KPVHPTESLP
LQGSAAWPLT QHELQKRGTS LGLSSSIIQH LGGAYGSNAN AVFDLIEQDA SLGQQLISDL
PYIKAEVIYA CRYEMAMKPS DILARRTSIV LEDRERGQGV VDEVTRLMAQ EFHWPSTEQQ
ALMQTYRSNI QNQVLAEKH
//
