ID A0A2P8F7Y1_9RHOB Unreviewed; 573 AA.
AC A0A2P8F7Y1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:PSL17830.1};
GN ORFNames=CLV88_11442 {ECO:0000313|EMBL:PSL17830.1};
OS Shimia abyssi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1662395 {ECO:0000313|EMBL:PSL17830.1, ECO:0000313|Proteomes:UP000240418};
RN [1] {ECO:0000313|EMBL:PSL17830.1, ECO:0000313|Proteomes:UP000240418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100673 {ECO:0000313|EMBL:PSL17830.1,
RC ECO:0000313|Proteomes:UP000240418};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PSL17830.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PYGJ01000014; PSL17830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8F7Y1; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000240418; 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: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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000240418}.
FT DOMAIN 19..368
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 417..537
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 573 AA; 62862 MW; EA22133071A2531B CRC64;
MSDQRQQTLT QLRSNADFDV VVIGGGVNGI GVYRELALQG LRVLLVERND FASGCSAAPS
RMIHGGLRYL ENGEFDLVRE SLQERDALLR NAPHMVHPLP TVIPITSTFS GVFNAAASFF
GGTGKPSSRG AVPIKLGLSL YDWVTRKRRV LPKHHFNTGA QTRRFWPALT DKATRSAVYH
DAQITHPERL CVEMIRDIAA TAPECAAFNY AEMHKDGAAY HVTDRRSDET LSVNPKVIVN
ATGAWLDDTV QSLGGGANET MVSGTKGSHL IIDNAALLNA LGEHMVYFEN TDGRVCIVFP
YQGKVLAGST DIRVDKATRV RCEPDERDYI LGSLRLVFPE IDVTPDQVVF SYSGIRPLPK
SDHDFTGRIS RGHDTRRLAG APVQFCMVGG KWTTFRAFAE QTGEMVLAEI GRERRLSTLN
LPIGGGAGFR ETPEVLARKL SDAFALSPNR AAHLIDHYGS NAHDVARFCL TQNDAPLISG
SPYSQAEISW LLRTEYIETL SDIALRRTAL AITGQMTSGV LDALSAILAQ ERDLSAESIK
QQQEALIHEL TEYYGVSPDA LTTGHNERRT ECA
//
