ID A0A0A0JDC8_9MICO Unreviewed; 568 AA.
AC A0A0A0JDC8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=N802_07400 {ECO:0000313|EMBL:KGN33636.1};
OS Knoellia sinensis KCTC 19936.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385520 {ECO:0000313|EMBL:KGN33636.1, ECO:0000313|Proteomes:UP000030002};
RN [1] {ECO:0000313|EMBL:KGN33636.1, ECO:0000313|Proteomes:UP000030002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 19936 {ECO:0000313|EMBL:KGN33636.1,
RC ECO:0000313|Proteomes:UP000030002};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia sinensis.";
RL Submitted (AUG-2013) 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:KGN33636.1}.
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DR EMBL; AVPJ01000003; KGN33636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0JDC8; -.
DR STRING; 1385520.N802_07400; -.
DR eggNOG; COG0578; Bacteria.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000030002; 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: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}.
FT DOMAIN 22..384
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..529
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 544..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 61715 MW; 2A0EA08100B2D9A2 CRC64;
MTLSPAARTS TLQRLRSGEE LDVLVVGGGV VGCGTALDAV TRGLSTGLIE ARDYASGTSS
RSSKLIHGGL RYLEMLDFGL VHEALQERRL LLTTIAPHLV RPVPFMYPLS KPAWERFYVG
SGIALYDGLA FGVRQTAGLP RHRHLGKKAA LRLMPSLRPD ALTGAIQYHD AQVDDSRFVL
ELARTAAMHG AHVVNRVAAV SMLRSEDGER VVGVRARDQR TGEEFDIRAR RVIAAAGVWT
DEIQSMLGEG GPLKVRASKG IHLVVPRDRI SSETGVILRT ARSVLFIIPW DEHWIIGTTD
TDWNLDKAHP AATSADIDYL LETVNSVLVT PLTRDDIDGV YAGLRPLISG DEADETTKLS
REHVVATPVP GLTLIAGGKY TTYRIMAKDA VDEAVQDFEA EVAASSTDKI PLAGAIGWEW
LSERPQILAR SAGIDQEHVE TLLERYGTLT KELIALINAQ PELGELLPGG ETHLKAEIVY
AAATEGAVHL TDILTRRTRI SIEARDRGII AAPHAAALAA PILGWDDARV AQELDIYHRR
VEAEMSSQTM PDDESAAEAR RLAPDATL
//
