ID A0A1A0THG4_9MYCO Unreviewed; 577 AA.
AC A0A1A0THG4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=A5757_18015 {ECO:0000313|EMBL:OBB58158.1};
OS Mycobacterium sp. 852013-51886_SCH5428379.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834111 {ECO:0000313|EMBL:OBB58158.1, ECO:0000313|Proteomes:UP000091910};
RN [1] {ECO:0000313|Proteomes:UP000091910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852013-51886_SCH5428379 {ECO:0000313|Proteomes:UP000091910};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL Submitted (JUN-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}.
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:OBB58158.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LZSU01000035; OBB58158.1; -; Genomic_DNA.
DR RefSeq; WP_066835373.1; NZ_LZSU01000035.1.
DR AlphaFoldDB; A0A1A0THG4; -.
DR STRING; 1834111.A5757_18015; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000091910; 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:UP000091910}.
FT DOMAIN 29..383
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"
SQ SEQUENCE 577 AA; 62809 MW; 69CBAC31A9253118 CRC64;
MREPGNDQTL LGPDQRTEAW QRLGSEQFDV VVIGGGVVGA GAALDAATRG LKVALVEARD
FASGTSSRSS KMFHGGLRYL EQLEFGLVRE ALHERELSLT TLAPHLVKPL PFLFPLTNRI
WERPYIAAGI FLYDQLGGAK SVPAQKHLTK AGALRLAPGL KRSSLIGGIR YYDTVVDDAR
HTMMVARTAA HYGAVVRTST QVVNMLREGD RVIGVVVRDS EDGAVTEVRG HVVVNATGVW
TDEIQALSKE RGRFRVRASK GVHVVVPRDR IVSEVAIILR TENSVLFVIP WGTHWIIGTT
DTDWNLDLAH PAATKADIDY ILGTVNTVLA TPLTHDDIDG VYAGLRPLLA GESEETSKLS
REHAVAVPAP GLVAIAGGKY TTYRVMAEDA IDAAAEFVPT RVAPSITEKV PLMGADGYFA
LINQTQHVGE QNGLHPYRVR HLLDRYGSLI GEVLALAEDR PELLTPITEA PVYLKVEAAY
AVVAEGALHL EDILSRRMRI SIEYPHRGVD CAREVAEVVA PLLGWSAEDV DREVDTYCAR
VDAEVRSQQQ PDDESADALR AAAPEARAEI LEPVPLT
//
