ID A0A238YJA7_9BACT Unreviewed; 540 AA.
AC A0A238YJA7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:SNR70489.1};
GN ORFNames=SAMN06269173_105240 {ECO:0000313|EMBL:SNR70489.1};
OS Hymenobacter mucosus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411120 {ECO:0000313|EMBL:SNR70489.1, ECO:0000313|Proteomes:UP000198310};
RN [1] {ECO:0000313|EMBL:SNR70489.1, ECO:0000313|Proteomes:UP000198310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28041 {ECO:0000313|EMBL:SNR70489.1,
RC ECO:0000313|Proteomes:UP000198310};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZNS01000005; SNR70489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238YJA7; -.
DR Proteomes; UP000198310; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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}.
FT DOMAIN 26..383
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 417..509
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 540 AA; 58974 MW; 4D2742896D92B371 CRC64;
MRNDTTTTRF QRSALLQQLT NQKSWDLIVI GGGATGLGVA LDGISRGYST LLLEQVDYAK
GTSSRSTKLV HGGVRYLAQG DVALVREALY ERGLLLKNAP HLVKNQDFII PNYEWWGGPF
YTIGLTMYDL LAGKLSLGAS KHLSKTETLR RLGNIKADGL KGGVLYHDGQ FDDARLAVNL
AQTAVERGGT LLNHFEVRGL LKDTQGKISG VMAADQETGT TYELTAKAVV NATGIFVDDI
LQMDKPGTKK LVRPSQGVHI VLDKSFLPGD DAIMIPKTDD GRVLFAVPWH NRVVLGTTDT
PLNEHSQEPQ ALEEEIDFIL RTAARYLTRA PKRSDALSIF AGLRPLAAPQ AGSEKTKEIS
RSHKILVSEA GLITITGGKW TTYRRMGQDT VDKAIALGKL PAAKSTTAQM PIHGAQPTPD
HSNHLYVYGT DQPALQQLIV QQPELGQKLD ASLEFLKAEV VWAARYEMAR TVEDVLARRV
RVLFLDAPAA IRMAPEVAAL LAQELGHDQR WEQQQVAAFT AVAQHYLLES QPAPVKAAAA
//
