ID F5XRQ2_MICPN Unreviewed; 565 AA.
AC F5XRQ2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:BAK37115.1};
GN OrderedLocusNames=MLP_41010 {ECO:0000313|EMBL:BAK37115.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK37115.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK37115.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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; AP012204; BAK37115.1; -; Genomic_DNA.
DR AlphaFoldDB; F5XRQ2; -.
DR STRING; 1032480.MLP_41010; -.
DR KEGG; mph:MLP_41010; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_11; -.
DR OMA; QKWWEAP; -.
DR Proteomes; UP000007947; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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:SF31; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 2; 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.
DR PROSITE; PS00977; FAD_G3PDH_1; 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 ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000007947}.
FT DOMAIN 8..369
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 391..516
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 565 AA; 60691 MW; A46F87B7F9ABFCA2 CRC64;
MSDDRGLDVL VIGGGVTGAG VALDAATRGL RVGVVDAQDW ASGTSSRSSK LVHGGLRYLQ
MLDFKLVSEA LGERGLLIDK LAPHLVRAVP FLYPLTKWYE RPYVGAGIAL YDALATFGTR
NRAVPLHRHV SRRGVREVFP GIKADVCRGA VRYYDGQVDD ARLVIALIRT AVQLGAYAAS
RTEVVELVKD DSGRVTGAVL RDLESGAEHL VRTRSVINAT GVWTEQTQSL VTDGGLHVLA
SKGIHIVVPR ERIAGTSGII LQTEKSVLFL IPWSRYWVIG TTDTAYHGDL THPVASHADI
DYVLDHANAI LAHPLTRNDV VGTWAGLRPL LQPGTKGDEK SSTKVSREHT VTEAAPGLVS
IAGGKLTTYR VMAEDAVDFA LGEQRATELP SETATTPLVG AAGYHAYARR ASEISRTYGW
SDATVAHLLH RYGSALSELL DLVDARPDLG RPLAGAEAYL RAEIVYGVSH EGALHLEDTM
TIRTRLTYEV GNHGLAAVTE IADLMAGQLG WDEARRQFEL DAYQARCAAE DAAAAAPDDE
AAQQARQRIG DVLADLPGAE VTTLA
//