ID A0A3G9ICK5_9ACTN Unreviewed; 588 AA.
AC A0A3G9ICK5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=Back2_09540 {ECO:0000313|EMBL:BBH16667.1};
OS Nocardioides baekrokdamisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1804624 {ECO:0000313|EMBL:BBH16667.1, ECO:0000313|Proteomes:UP000271573};
RN [1] {ECO:0000313|EMBL:BBH16667.1, ECO:0000313|Proteomes:UP000271573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 39748 {ECO:0000313|EMBL:BBH16667.1,
RC ECO:0000313|Proteomes:UP000271573};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Shin Y.K., Lee J.S.;
RT "Complete genome sequence of Nocardioides baekrokdamisoli strain KCTC
RT 39748.";
RL Submitted (NOV-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}.
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DR EMBL; AP019307; BBH16667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9ICK5; -.
DR KEGG; nbe:Back2_09540; -.
DR Proteomes; UP000271573; Chromosome.
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:UP000271573}.
FT DOMAIN 29..391
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 417..541
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 588 AA; 64040 MW; 75F24AC912D870EC CRC64;
MTTLGAMDAA QRESAIAALA GTAGEPELDV LVVGGGIVGA GVALDAVTRG LNTGLVEQRD
LASGTSSRSS KLVHGGLRYL EMLDFGLVRE ALQERGLLVT KLAPHLVRPV PFLYPLTHPV
WERGYVGSGL LLYDAMAAVG KHSGLGQMGL PRHRHLGKRA VQRIAPDFRS DAITGAIQYY
DAQVDDARLV TTIARTAARH GAQIATRTQV IGFVREGERV VGVRAKDLES GVEFVIRARV
VVNAAGVWTD DIQELVGGRG SLHVQASKGI HLVVPRDRIR SESGFIVRTE KSVLFVIPWG
RHWIIGTTDT PWTYDKAHPA ATRADIDYLL GHVNAILREP LDHEDVEGVY AGLRPLLTGQ
SDSTAKLSRE HTVVTPVPGL VMIAGGKLTT YRVMAKDAVD AAVHSLKTTT DQAIQESITD
KVRLLGAENF ETRSNQRVLL ARRSGLHVAR IDHLLGRYGG LIDEVLDLIH HRRALALPLE
GAEDYLAAEV VYAVTHEGAV HLDDVLVRRT RISMETFDRG VAAAPAAARL MAQELGWDAE
RVRAEVEHYL ERVTAERASQ QMVTDAAADE VRLQARDHLR EEARPKGR
//
