ID A0A1Y5XCN6_KIBAR Unreviewed; 586 AA.
AC A0A1Y5XCN6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN05661093_02327 {ECO:0000313|EMBL:SMC86190.1};
OS Kibdelosporangium aridum.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=2030 {ECO:0000313|EMBL:SMC86190.1, ECO:0000313|Proteomes:UP000192674};
RN [1] {ECO:0000313|EMBL:SMC86190.1, ECO:0000313|Proteomes:UP000192674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43828 {ECO:0000313|EMBL:SMC86190.1,
RC ECO:0000313|Proteomes:UP000192674};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXV01000002; SMC86190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5XCN6; -.
DR Proteomes; UP000192674; 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; 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:UP000192674}.
FT DOMAIN 40..393
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 416..539
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 64143 MW; 431A156C82E9B489 CRC64;
MASRKPRQPV RTIDPVTVPG RLGPAEREDS WRRLGEETFD LVVIGGGVVG AGTALDAATR
GLRVALVEAR DLASGTSSRS SKLFHGGLRY LEQLEFGLVR EALRERELML TRIAPHLVKP
VSFLYPLTRR VWERPYTAAG LFLYDTMGGA RSVPGQKHLT RAGALRMVPA LKRDALIGGI
RYFDAQSDDA RHTMTVARTA AHYGAVVRTS TQVIGMVREA DRISGVRVRD VEDGRETEIK
ANAVINATGV WTDELQRLSG SRGRFRVRAS KGVHIVVPRD RIVSESGLIL RTEKSVLFVI
PWGSHWIVGT TDTDWNLDLA HPAATKADID YILEHVNTVL ATPLTQDDIE GVYAGLRPLL
AGESEETSKL SREHAVARVA PGFVAIAGGK YTTYRVMAAD AVDAAAVDLP GRIQPSITDK
VPLLGADGYH ALVNQADQLA AKAGVHPYRV RHLLNRYGSM IHQLLALAEN RPELLKPLTA
APDYLQVEVV YATSHEGALH LEDVLARRTR ISIEYAHRGV DAAEQVAALM AEILGWDEAA
MKREVELYTA RVQAERDSQT QPNDEAADAL RSKAPEARAQ ITEPVS
//
