ID A0A2V1K866_9ACTO Unreviewed; 570 AA.
AC A0A2V1K866;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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 ORFNames=DD236_05970 {ECO:0000313|EMBL:PWF26406.1};
OS Ancrocorticia populi.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Ancrocorticia.
OX NCBI_TaxID=2175228 {ECO:0000313|EMBL:PWF26406.1, ECO:0000313|Proteomes:UP000245283};
RN [1] {ECO:0000313|Proteomes:UP000245283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sk1b4 {ECO:0000313|Proteomes:UP000245283};
RA Li Y.;
RL Submitted (MAY-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:PWF26406.1}.
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DR EMBL; QETB01000003; PWF26406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1K866; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000245283; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245283}.
FT DOMAIN 22..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 407..531
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 549..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 61502 MW; F0796FF4658FD60E CRC64;
MSVLSLEQRA SSLEALQDGE YDVLVVGGGV TGAGIALDAA SRGLRTAVIE AQDWASGTSS
RSSRLVHGGL RYLYNLDFKL VAEALRERGN LLTTIAPHLV EAQPFLWPLK TPVIERAYSA
VGVGMYDALA VAGAGGHKTV PIQQHHTKKG ALKRFPEIKP SALNGAIEFY DARVDDARLV
ITLIRTALSY GAEAASRTRV HEFLKDSRGH AAGVVATDLE TGNEITVHAK RVINATGIWT
EETQDMAGGT GGLKVLASKG VHIVIPRERF TAQTGIFLRT EKSVLFIIPW QHYWVIGTTD
TAWHEQLKHP VPTSEDIDYI LEQANKILDR PLTREDIIGT YAGLRPLLQP KVLDESKSTK
VSREHTVTEV IPGMVAIAGG KLTTYRVMAE DAVDFALGEE EAKRRPSVTS SLPLAGAAGY
QAAVNQSERL GAKYGFDADR MKHLLSRYGS EIGEVLATID EDPTLATPLE AAPQFIRAEV
HRACTVEGAL HLEDIFVARV RLNSEARDRG GAAVDEIAEI AAAALGWSAE QTEAEKDNYR
ARIASELAAE AQSNDAAASA ERTQAPDIVG
//
