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Database: UniProt
Entry: A0A1K1SIR8_9PSEU
LinkDB: A0A1K1SIR8_9PSEU
Original site: A0A1K1SIR8_9PSEU 
ID   A0A1K1SIR8_9PSEU        Unreviewed;       562 AA.
AC   A0A1K1SIR8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=SAMN04489730_5718 {ECO:0000313|EMBL:SFW83781.1};
OS   Amycolatopsis australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW83781.1, ECO:0000313|Proteomes:UP000182740};
RN   [1] {ECO:0000313|EMBL:SFW83781.1, ECO:0000313|Proteomes:UP000182740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW83781.1,
RC   ECO:0000313|Proteomes:UP000182740};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FPJG01000006; SFW83781.1; -; Genomic_DNA.
DR   RefSeq; WP_072479162.1; NZ_FPJG01000006.1.
DR   AlphaFoldDB; A0A1K1SIR8; -.
DR   STRING; 546364.SAMN04489730_5718; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000182740; 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:SF31; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 2; 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}.
FT   DOMAIN          22..371
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          399..523
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          539..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  61148 MW;  06E1834BEEE57EB1 CRC64;
     MTPLSPQYRA ETLRKLVDEE IDVLVVGGGV TGAGVALDAA SRGLSTALVE ARDFAAGTSS
     RSSKLIHGGL RYLEQLDFKL VREALKERGL LLQKLAPHLV RPVKFLVPLQ HRVWERGYIG
     AGVTLYDTLG GARALPRHRH LSKRGAFKVA PGLADDALIG AIQYYDAQVD DARHTMTIAR
     TAAEQGASVL TRTRVTSLLR AGERVVGAKV VDRESGVEFE IRAKTVVAAT GVWSDDMAEA
     AGIPAPFTVR ASKGIHLVVP REKIDLDTGL ILRTEKSVLF VIPWGRHWIV GTTDTEWDLD
     REHPAASRAD VDYVLDHLNA VLRTPVTHDD IEGVYAGLRP LLAAKATATT KLSREHAVAR
     PVPGLVIVAG GKYTTYRVMA ADAVDAAVEE VGRPAPPSWT DRLPIVGAEG YHELWEDRFS
     LASRTGLPLP RVEHLLQRYG TRIWNLVDLI EAEPGLAQPI TDTSDYLRVE AVYAVSHEGA
     LHLEDVLTRR TRISIEERDR GVAAAPVVAG LIAPLLGWDE HKREREVANY LARVEAERSA
     QEAPDDAAAN ATRLAAPALL PS
//
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