ID A0A0M4KKN4_9BURK Unreviewed; 611 AA.
AC A0A0M4KKN4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ALD91012.1};
GN Name=glpD {ECO:0000313|EMBL:ALD91012.1};
GN ORFNames=CR3_1794 {ECO:0000313|EMBL:ALD91012.1};
OS Cupriavidus gilardii CR3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1267562 {ECO:0000313|EMBL:ALD91012.1};
RN [1] {ECO:0000313|EMBL:ALD91012.1, ECO:0000313|Proteomes:UP000067663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR3 {ECO:0000313|EMBL:ALD91012.1,
RC ECO:0000313|Proteomes:UP000067663};
RX PubMed=26301592;
RA Wang X., Chen M., Xiao J., Hao L., Crowley D.E., Zhang Z., Yu J., Huang N.,
RA Huo M., Wu J.;
RT "Genome Sequence Analysis of the Naphthenic Acid Degrading and Metal
RT Resistant Bacterium Cupriavidus gilardii CR3.";
RL PLoS ONE 10:E0132881-E0132881(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR EMBL; CP010516; ALD91012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4KKN4; -.
DR STRING; 1267562.CR3_1794; -.
DR KEGG; cgd:CR3_1794; -.
DR PATRIC; fig|1267562.4.peg.2112; -.
DR Proteomes; UP000067663; Chromosome 1.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 26..386
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 434..497
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 502..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..598
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 66561 MW; 25ADBBAD43FF2427 CRC64;
MQTPNPTLPP DRAALLAALE RERRWDVIVI GGGATGLGTA VDAASRGYRT LLLEAADFAK
GTSSKATKLV HGGVRYLAQG NIGLVREALQ ERGMLARNAP HLVWPLGFVV PAYQLFDQPF
YGIGLKVYDM LAGSRNLMDS RWLNHQQALA AAPTLAEHVG GRPLRGANLY FDGQFDDARL
AIALMRTLFD LGGVALNYAR VTGLVMQAGV VGGVTVRDAL GDAELTLHAE CVINATGVWV
DAVRRMEDER AQMMVAPSQG VHLTLPRSFL PGDRAILVPK TDDGRVLFLV PWNGHTIVGT
TDTPRRDLPL EPRAEDDDVD FILETAARYL SRDPTRDDVT SVWAGLRPLV KATGESSTAS
LSREHTIVVS KAGLITVTGG KWTTYRKMAE DVIDTAIRRQ MLRAAPCVTA DLPLHGAGAW
AGQQANLNAP DRYYGGDLGL LRSLPGADNV LAPESGLTEA HVRFAARYEL ARKVEDVVAR
RNRLLFLDAR AAEAAARAWR RSSPKNWGTT PPGSRRRSTA CASSRPAIGS MPAGNVERHA
RRACSSIPST ALCRTNRYGH LPALCPRRPA SRRRAARRRL RRGRLRRAGT GPSRHRRRAL
RCAGHRALPL R
//
