ID A1R6X8_PAEAT Unreviewed; 593 AA.
AC A1R6X8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ABM06900.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:ABM06900.1};
GN Name=glpD {ECO:0000313|EMBL:ABM06900.1};
GN OrderedLocusNames=AAur_2249 {ECO:0000313|EMBL:ABM06900.1};
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paenarthrobacter.
OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM06900.1, ECO:0000313|Proteomes:UP000000637};
RN [1] {ECO:0000313|EMBL:ABM06900.1, ECO:0000313|Proteomes:UP000000637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1 {ECO:0000313|EMBL:ABM06900.1,
RC ECO:0000313|Proteomes:UP000000637};
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM06900.1; -; Genomic_DNA.
DR RefSeq; WP_011774934.1; NC_008711.1.
DR AlphaFoldDB; A1R6X8; -.
DR STRING; 290340.AAur_2249; -.
DR KEGG; aau:AAur_2249; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_11; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000000637; 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:ABM06900.1}.
FT DOMAIN 28..379
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 445..568
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 593 AA; 64710 MW; 5FA7215A2F5DF0F4 CRC64;
MGHNRISGTS QHTQRDSVVA LQERPSAKVL IIGGGINGVG TFRDLALQGV DVALVERGDY
CQGASGASSH MIHGGIRYLE NGEFRLVQES VVERNRLLRI APHYVKPLQT TIPIFSTFSG
ILSAPMRFLT HKQGKPKERG AFLIKVGLSM YDFFSRDGGS VPRHQFRGRT KALAELPKLH
SGIKYAATYF DASVHNPERL TLDVLQDGEK AGRGGGLPGG SARASNYVSL VSMGSDGVRL
RDELTGKEFD FQADVIVNTT GAWVDLTNQA MGAVSKFMGG TKGSHIVLDH PELLAACNGR
EIFFEHTDGR IVLIYPMGDR VLVGTTDVDA DMSEDAVCTD EEIDYFFDLV GHVFPTIKVE
REQIVYSFAG VRPLPRHDET QPGFVSRDYR IERSVRTGGD AVPTPGGKAA VVLSLVGGKW
TTFRALAEHM SNDVLRELGM ERKVSTAKLA IGGGAGFPAS EQGEQEWIKK HMGPGLDADR
VAVLLTRYGT RADAVIDYLN AGHDTPLRST RELSVRELAF MAEHEQIGHL VDVLIRRTSL
AFRGLVTGEL LNEIAAALAE PLGWDAAARE AEIRHAQEVL QRFHKVDVHS LVA
//
