GenomeNet

Database: UniProt/TrEMBL
Entry: E6XE22_CELAD
LinkDB: E6XE22_CELAD
Original site: E6XE22_CELAD 
ID   E6XE22_CELAD            Unreviewed;       549 AA.
AC   E6XE22;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Homodimeric glycerol 3-phosphate dehydrogenase (Quinone) {ECO:0000313|EMBL:ADV48088.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:ADV48088.1};
GN   OrderedLocusNames=Celal_0753 {ECO:0000313|EMBL:ADV48088.1};
OS   Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV48088.1, ECO:0000313|Proteomes:UP000008634};
RN   [1] {ECO:0000313|EMBL:ADV48088.1, ECO:0000313|Proteomes:UP000008634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14237 / IC166 / ACAM 630
RC   {ECO:0000313|Proteomes:UP000008634};
RX   PubMed=21475589; DOI=10.4056/sigs.1543845;
RA   Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL   Stand. Genomic Sci. 4:72-80(2010).
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; CP002453; ADV48088.1; -; Genomic_DNA.
DR   RefSeq; WP_013549578.1; NC_014934.1.
DR   AlphaFoldDB; E6XE22; -.
DR   STRING; 688270.Celal_0753; -.
DR   KEGG; cao:Celal_0753; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_10; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000008634; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADV48088.1}.
FT   DOMAIN          24..377
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          408..531
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   549 AA;  61860 MW;  5BCA7AC4FED073F2 CRC64;
     MKKENFTYLK RDKITEELKA NTFDLVVIGG GITGAGILLD ASSRGMKVAL IEKGDFASGT
     SSKSSKLIHG GLRYLKQFEL MLVKEVGTER AIVHKLAPHL VIPEKMLLPL IEDGSYGEWM
     TSIGLKVYDI LADVEGDDKR KMMNKEETLA LEPLLPEGIL KGSGYYAEYR TDDARLTLEN
     IKTALNYNAT AINYTKVTDF LYDGDQISGV TVTDAVSGES YQIHSKYVIN AAGPWVDELR
     TINHSKEGKQ LHLTKGVHLV FEKAKLPLKQ SVYFDIPDGR MMFAIPRGNV TYAGTTDTNY
     KHSKEDVVAT VEDADYLLDA INNMFPSVHL ERKDIVSSWA GLRPLIHEEG KSPSELSRKD
     EIFNSDSGLL SMAGGKLTGY RKMAERVVDK VHKKLEKQTS ARFKDVFTDK IPLTGGPWKK
     YKEVKKYITK INDILEKDNF EAHEAWYLVT TYGKQTEAIL QIYASSTGAN PKENLIMAEL
     EFCMHHEMVV TPLDFFIRRT GRLYFNIESV KAYREKVFAV FKETFALSEE TLSAYNSELD
     ALIKSHSEF
//
DBGET integrated database retrieval system