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Database: UniProt
Entry: F5XRQ2_MICPN
LinkDB: F5XRQ2_MICPN
Original site: F5XRQ2_MICPN 
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}.
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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
//
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