ID GLPB_ACTP7 Reviewed; 428 AA. AC B3H0P4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753}; DE Short=Anaerobic G-3-P dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753}; DE Short=Anaerobic G3Pdhase B {ECO:0000255|HAMAP-Rule:MF_00753}; DE EC=1.1.5.3 {ECO:0000255|HAMAP-Rule:MF_00753}; GN Name=glpB {ECO:0000255|HAMAP-Rule:MF_00753}; GN OrderedLocusNames=APP7_0404; OS Actinobacillus pleuropneumoniae serotype 7 (strain AP76). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=537457; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AP76; RA Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N., RA Tegetmeyer H., Singh M., Gerlach G.F.; RT "Genome and proteome analysis of A. pleuropneumoniae serotype 7."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses CC fumarate or nitrate as electron acceptor. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00753}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC 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:0000255|HAMAP-Rule:MF_00753}. CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound CC GlpC. {ECO:0000255|HAMAP-Rule:MF_00753}. CC -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B CC family. {ECO:0000255|HAMAP-Rule:MF_00753}. 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; CP001091; ACE61056.1; -; Genomic_DNA. DR RefSeq; WP_005611546.1; NC_010939.1. DR AlphaFoldDB; B3H0P4; -. DR KEGG; apa:APP7_0404; -. DR HOGENOM; CLU_047793_0_0_6; -. DR UniPathway; UPA00618; UER00673. DR Proteomes; UP000001226; 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; 2. 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 PANTHER; PTHR43400:SF11; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1. DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 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; FMN; Oxidoreductase. FT CHAIN 1..428 FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit FT B" FT /id="PRO_1000133353" SQ SEQUENCE 428 AA; 46784 MW; 6602C65C34B60043 CRC64; MNFDVVIIGG GLAGLTCGIA LQEQGKRCVI INNGQAAIDF SSGSMDLLSR LPSGQKVENV YQSLDELKLQ APEHPYSILG KDQVLAKAQQ FEQLAQSLNL HLEGSTVQNH ERITPLGGLR ATWLSPNSVP TVKHLTALAD KQVAILGIEG YHDFQPQLLA DNLKQHSQFA DYEFTIGYLN IPELDYLRQN SREFRSVNIA QLLEHKLSFQ DLVQEIKQAA GNAKAVFLPA CFGLDNQDFF NSLQQATGLA LFELPTLPPS LLGIRQHRQL RSRFEQLGGM MMNGDRAVKA EFEGKNVARI FTTSHQEEPI SADYFVLAAG SFFSNGLVAE FERVKEPVFD LDICGCKNFD SSDRFTWTNN RFAAPQPYQS AGVVINSACQ VQKNGEVVSN LYAVGNVIGG FQGIEQGCGS GVAVVTALTV AEQIGGTK //