ID A0A1K1S5W5_9BACT Unreviewed; 520 AA.
AC A0A1K1S5W5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:SFW79824.1};
GN ORFNames=SAMN05661012_04843 {ECO:0000313|EMBL:SFW79824.1};
OS Chitinophaga sancti.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW79824.1, ECO:0000313|Proteomes:UP000183788};
RN [1] {ECO:0000313|EMBL:SFW79824.1, ECO:0000313|Proteomes:UP000183788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 784 {ECO:0000313|EMBL:SFW79824.1,
RC ECO:0000313|Proteomes:UP000183788};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
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; FPIZ01000018; SFW79824.1; -; Genomic_DNA.
DR RefSeq; WP_072363806.1; NZ_FPIZ01000018.1.
DR AlphaFoldDB; A0A1K1S5W5; -.
DR STRING; 1004.SAMN05661012_04843; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000183788; 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 17..371
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 368..501
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 520 AA; 57037 MW; ACD866A25398A305 CRC64;
MNRMQLISDL SSTKSWDVIV IGGGATGLGI AMDAATRGYK TLLVEQADYS KGTSSKATKL
VHGGVRYMAQ GDLGLVKEAC HERGLLLKNA PHLTKNETFV IPNYSLFNNL KYTIGLKFYD
LLAGKLSLGA SKYISKKKTI EALPTIRQEG LKGGVVYHDG QFDDSRLALN IAQTAIENGA
TVLNYVKVTG LLKDNNKKVN GIIAKDIETG ETYEATGKVV INATGVYVDN ILHMDRPDAP
HMVRPSQGVH ITLDHSFLPG DNALMIPETD DGRVLFAVPW HGKLIVGTTD TLRDHPELEP
HALEQEIEFI LNTAAKYLVK KPTRKDVLAV FAGLRPLAAP GKDGAKTKEI SRSHKIIVSE
SGLITITGGK WTTFRRMAQD TIDKAIETGV LPAKECKTEH LPIHGYVQAS DEKDPLRFYG
ADMTAINQLV AADPSLGELL VPNFPYNKAM VIWAIRNEYA RRVEDILGRR LRLLFLDVHA
AIAAAPVVAQ LLARELNKDA AWIQAELKDF EILAKGYTLN
//
