ID J3D369_9BURK Unreviewed; 529 AA.
AC J3D369;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:EJL83606.1};
GN ORFNames=PMI15_02619 {ECO:0000313|EMBL:EJL83606.1};
OS Polaromonas sp. CF318.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL83606.1, ECO:0000313|Proteomes:UP000007275};
RN [1] {ECO:0000313|EMBL:EJL83606.1, ECO:0000313|Proteomes:UP000007275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF318 {ECO:0000313|EMBL:EJL83606.1,
RC ECO:0000313|Proteomes:UP000007275};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
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:EJL83606.1}.
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DR EMBL; AKIV01000065; EJL83606.1; -; Genomic_DNA.
DR RefSeq; WP_007869244.1; NZ_AKIV01000065.1.
DR AlphaFoldDB; J3D369; -.
DR PATRIC; fig|1144318.3.peg.2550; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000007275; Unassembled WGS sequence.
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 27..389
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 413..512
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 529 AA; 56573 MW; A8CFF3DDDFF9E59F CRC64;
MSTEFVPAAA TRRQDLMDSL AAPRHYDIAI IGGGATGLGV ALDAAARGFS VVLVESHDFA
KGTSSRATKL VHGGVRYLAQ GNISLVREAL LERTTLLANA PHLAQPLPFV MPSYKFWEAP
FYGIGLKMYD ALAGKAGLGA TEFLNRRETL AYLPTVQPRD LKGGVKYWDG QFDDARLALA
LARTAASQGA LLVNYCAATG LIHEGGKLAG LHACDQETGR TFEIRASCVV NAAGVWVDQL
RLLDGQAIGR DTKPMVAPSQ GVHIVVDRSF LPTDHALLVP KTADGRVLFA VPWLGKTILG
TTDTPRHDLA REPLPFREEV DFILRESARY LSRAPGPADI KSIWVGLRPL VKPPDDDAGS
TQALSREHTV LVSKSGLVTV TGGKWTTYRA MAEDVLDKCF GASLLPARAG STTAHLKLVG
AHNSGHKISE APGPHLYGSE AASLDSLPGA GRELGGGLTE AMVRFAARHE YARTVEDVLA
RRSRLLFLDA ALARTLAPEV ATLLQQENGV DPQLDAFLAL CGQYLSLPD
//
