ID K9DCB5_9BURK Unreviewed; 536 AA.
AC K9DCB5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9710_02352 {ECO:0000313|EMBL:EKU82329.1};
OS Massilia timonae CCUG 45783.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU82329.1, ECO:0000313|Proteomes:UP000009874};
RN [1] {ECO:0000313|EMBL:EKU82329.1, ECO:0000313|Proteomes:UP000009874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU82329.1,
RC ECO:0000313|Proteomes:UP000009874};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Massilia timonae CCUG 45783.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EKU82329.1}.
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DR EMBL; AGZI01000027; EKU82329.1; -; Genomic_DNA.
DR RefSeq; WP_005666626.1; NZ_JH992923.1.
DR AlphaFoldDB; K9DCB5; -.
DR STRING; 47229.LO55_3073; -.
DR PATRIC; fig|883126.3.peg.2384; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_4; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000009874; 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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009874}.
FT DOMAIN 14..382
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 417..514
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 128..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 58414 MW; 7DECC46E73CF9DBF CRC64;
MSGANVFPPG RDWDLLVIGG GITGAGILLE AARRDLKTLL VEQKDFAWGT SSRSSKLVHG
GLRYLASGDL RLTRDAVRER ESLLRAAPGL VEPQGFAFAD HGTDVKRRLG FLSMLRVYEV
LAGRREPRWE RPESSRMPSP NSPEANPAGG IRYTDAKTDD ARLVLRVIDE ARAHGAVACN
YVTVQALVRD GGKVHGAMLR DERSQAETAV RARVVVNATG AWSDLLGGAA GGEAGGKAGG
KAGSTKPDRA PRLRPLRGSH LVLPARRLPL AQAVSLLHPA DSRPVFAFPW EGVTLVGTDA
DHEQGLNTEP RITRPEFDYL MAALHAQFPQ LGLSEQDVVA TFAGVRPVID GGQHGAPSSE
KRDHFVWSEP GLVSVAGGKL TTFRAIALDV LRHVSQQLPG WQLRAERGPV FARVSVPARH
DLPPGVLRRL AGRYGAQAKP LLLAARKGEL ECIPGTQTLW AELRWAARSE QVYQLDDLLL
RRTRLGIQLP NGGLDQMTRI RAICQPELGW DDARWEAQER RYLAEWGKQY GVPPVA
//
