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Database: UniProt
Entry: L0M3W3_ENTBF
LinkDB: L0M3W3_ENTBF
Original site: L0M3W3_ENTBF 
ID   L0M3W3_ENTBF            Unreviewed;       419 AA.
AC   L0M3W3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B {ECO:0000256|HAMAP-Rule:MF_00753};
DE            Short=Anaerobic G-3-P dehydrogenase subunit B {ECO:0000256|HAMAP-Rule:MF_00753};
DE            Short=Anaerobic G3Pdhase B {ECO:0000256|HAMAP-Rule:MF_00753};
DE            EC=1.1.5.3 {ECO:0000256|HAMAP-Rule:MF_00753};
GN   Name=glpB {ECO:0000256|HAMAP-Rule:MF_00753};
GN   OrderedLocusNames=D782_1408 {ECO:0000313|EMBL:AGB77421.1};
OS   Enterobacteriaceae bacterium (strain FGI 57).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB77421.1, ECO:0000313|Proteomes:UP000011002};
RN   [1] {ECO:0000313|EMBL:AGB77421.1, ECO:0000313|Proteomes:UP000011002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI 57 {ECO:0000313|EMBL:AGB77421.1,
RC   ECO:0000313|Proteomes:UP000011002};
RX   PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA   Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA   Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA   Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA   Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA   Currie C.R.;
RT   "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT   associated with leaf-cutter ant fungus gardens.";
RL   Genome Announc. 1:E00238-12(2013).
CC   -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC       fumarate or nitrate as electron acceptor. {ECO:0000256|HAMAP-
CC       Rule:MF_00753}.
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|HAMAP-Rule:MF_00753};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00753};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00753}.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC. {ECO:0000256|HAMAP-Rule:MF_00753}.
CC   -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC       family. {ECO:0000256|HAMAP-Rule:MF_00753}.
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DR   EMBL; CP003938; AGB77421.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0M3W3; -.
DR   STRING; 693444.D782_1408; -.
DR   KEGG; ebf:D782_1408; -.
DR   PATRIC; fig|693444.3.peg.1350; -.
DR   eggNOG; COG3075; Bacteria.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OrthoDB; 6395323at2; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000011002; Chromosome.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   HAMAP; MF_00753; Glycerol3P_GlpB; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR009158; G3P_DH_GlpB_su.
DR   NCBIfam; TIGR03378; glycerol3P_GlpB; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_00753};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00753};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00753}; Reference proteome {ECO:0000313|Proteomes:UP000011002}.
FT   DOMAIN          4..399
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   419 AA;  45294 MW;  72350ACFCB90D9F3 CRC64;
     MKFDTVIIGG GLAGLLCGLK LQSQGLRCAI VSRGQSALNF ASGSLDLLSM LPDGQPVEDI
     HLGLEALRRQ APEHPYNKVG CENVLSYARQ AQALFSECGI DFQGEAEQSH QRVTPLGLLR
     SAWLSPRETP LFPPAASKVR VVGITGFLDF QAPLAAESLR KQGLDVDTVE IDLPQLDVLR
     ENASEFRAAN IARLLDQPEQ WQPLYDALAP LAQGCDALWL PACFGASDSQ LYDWLCGKLS
     CALHLLPTLP PSVPGMRLQA QLQRQFIRAG GVWMPGDEVQ KVTLENQLAT AVWTRNHADI
     PLRARYVVLA SGSFFSNGLI ANRETIREPV LNLDVMQAAT RVLWYRPDVF DPQPWQQFGV
     ATDATLRPAI AGQRLENLFV IGSVLGGCDA IAQGCGGGVC AVTALHAAQQ IALLMGGEA
//
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