ID A0A0D1LHX2_9MYCO Unreviewed; 581 AA.
AC A0A0D1LHX2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=TL10_18185 {ECO:0000313|EMBL:KIU15616.1};
OS Mycolicibacterium llatzerense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU15616.1, ECO:0000313|Proteomes:UP000032221};
RN [1] {ECO:0000313|EMBL:KIU15616.1, ECO:0000313|Proteomes:UP000032221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLUC14 {ECO:0000313|EMBL:KIU15616.1,
RC ECO:0000313|Proteomes:UP000032221};
RA Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT recovered from brain abscess.";
RL Submitted (JAN-2015) 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:KIU15616.1}.
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DR EMBL; JXST01000025; KIU15616.1; -; Genomic_DNA.
DR RefSeq; WP_043986699.1; NZ_LXSC01000001.1.
DR AlphaFoldDB; A0A0D1LHX2; -.
DR STRING; 280871.TL10_18185; -.
DR PATRIC; fig|280871.6.peg.3761; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000032221; 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.
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:UP000032221}.
FT DOMAIN 33..387
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 409..533
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 581 AA; 63263 MW; E8CA86139EE4E12D CRC64;
MSDPIPGPGN GQTLLNRAQR ETAWNRLGSE QFDVIVIGGG VVGAGAALDA ATRGLKVALV
EARDFASGTS SRSSKMFHGG LRYLEQLEFG LVREALYERE LSLTTLAPHL VKPLPFLFPL
TKRIWERPYI AAGIFLYDQL GGAKSVPAQK HLLKAGALRL APGLKRSSLV GAIRYYDTVV
DDARHTMTVA RTAAHYGAVV RTSTQVVALL REGDRVTGVR IRDSETGAVT EVCGHVVVNA
TGVWTDEIQA LSKQRGRFRV RASKGVHIVV PRDRIVSEVA IILRTEKSVL FVIPWGTHWI
IGTTDTDWNL DLAHPAATKA DIDYILGHVN KVLATPLNHD DIDGVYAGLR PLLAGESEET
SKLSREHAVA VPAPGLVAIA GGKYTTYRVM GEDAIDAASE FVPTRVAPSI TEKVPLLGAD
GYFALINQTE HVGQHYGLHP YRVRHLLDRY GSLIGEVLDM AADRPELLEP ITEAPVYLKV
EAWYAAAAEG ALHLEDILAR RMRISIEYQH RGVDCAREVA EVIAPVLGWS AEDIDREVAT
YLARVEAEVL SQTQPDDESA DALRAAAPES RAEILEPVPL D
//
