ID   E1VWB4_GLUAR            Unreviewed;       559 AA.
AC   E1VWB4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:CBT75917.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:CBT75917.1};
GN   Name=glpD {ECO:0000313|EMBL:CBT75917.1};
GN   OrderedLocusNames=AARI_17030 {ECO:0000313|EMBL:CBT75917.1};
OS   Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS   JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Glutamicibacter.
OX   NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN   [1] {ECO:0000313|EMBL:CBT75917.1, ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RX   PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA   Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA   Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA   Vallaeys T.;
RT   "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT   adaptation to the surface of cheese.";
RL   PLoS ONE 5:E15489-E15489(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC   {ECO:0000313|Proteomes:UP000006878};
RA   Genoscope.;
RT   "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT   CIP 108037 / JCM 13566 / Re117).";
RL   Submitted (JUL-2010) 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; FQ311875; CBT75917.1; -; Genomic_DNA.
DR   RefSeq; WP_013349047.1; NC_014550.1.
DR   AlphaFoldDB; E1VWB4; -.
DR   STRING; 861360.AARI_17030; -.
DR   KEGG; aai:AARI_17030; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   Proteomes; UP000006878; 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: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   ECO:0000313|EMBL:CBT75917.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006878}.
FT   DOMAIN          16..359
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          417..538
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   559 AA;  61705 MW;  8BFEAFA211C47D55 CRC64;
     MIREQLAKLR ERPQAKVLVV GGGINGVATF RYLAMQGIDV ALIERGDYCQ GASGASSHMI
     HGGIRYLENG EFRLVHESVQ ERNSLLEIAP HYVKPLQTTI PIFSTFSGIL SAPMRFLTHK
     SGKPTERGAA LIKAGLIMYD VFAGIGGRNT PWHNFKAGKA AREDLPELRD DVKYTATYFD
     ASVHNPERLT LDVLREGLNA NDQARASNYV ELTGVESGIA KLRDVLSGEE FDFDAEVIIN
     ATGAWVDMTN QDLGRETKWT GGTKGSHIVL DHPELLAATG GREIFFEHED GRIVLIYPML
     GRVLVGTTDL EHDMNEPAVC TDEEVEYFFD LVHHVFPGIK ATEEQIVYKF SGVRPLPSHD
     DTAPGFVSRD YQIKETRLTD TTTMLSLIGG KWTTFRALSE NLGGKALEFL GAREVKSTAG
     VAIGGGKNFP RNDGEVAAWF AARESRAGRE RLRILLERYG TGADALLEAI GENETLLEHT
     KELSCEELAY MANYEQVGRL IDVFIRRTNL AFRGLVTKNL VIEVANCLAD PMGWDKSQIQ
     AEIDHSVSVL ADSHGVLLD
//