ID GLPB_ALIF1 Reviewed; 455 AA. AC Q5E0X7; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 99. 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=VF_A0249; OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Aliivibrio. OX NCBI_TaxID=312309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700601 / ES114; RX PubMed=15703294; DOI=10.1073/pnas.0409900102; RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., RA Stevens A., Visick K., Whistler C., Greenberg E.P.; RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with RT pathogenic congeners."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005). 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; CP000021; AAW87319.1; -; Genomic_DNA. DR RefSeq; WP_011263143.1; NC_006841.2. DR RefSeq; YP_206207.1; NC_006841.2. DR AlphaFoldDB; Q5E0X7; -. DR STRING; 312309.VF_A0249; -. DR EnsemblBacteria; AAW87319; AAW87319; VF_A0249. DR KEGG; vfi:VF_A0249; -. DR PATRIC; fig|312309.11.peg.2853; -. DR eggNOG; COG3075; Bacteria. DR HOGENOM; CLU_047793_0_0_6; -. DR OrthoDB; 6395323at2; -. DR UniPathway; UPA00618; UER00673. DR Proteomes; UP000000537; Chromosome II. 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; FMN; Oxidoreductase; Reference proteome. FT CHAIN 1..455 FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit FT B" FT /id="PRO_0000258910" SQ SEQUENCE 455 AA; 49930 MW; B1425B3B3BB5CD54 CRC64; MNFDTIIIGG GMAGLSCALR CLEAGLKTAV IASGQSALHF SSGSIDVLAK TPSGKHVINP MDSLETFSKE YPSHPYAALG KETVERAINW YKTTLSAIGV PLTSQKDGLN HYRLTPLGTM KSTWLSQPFV HQFPMDLEKN KTQKMVLITI DGFRDFQPKL AQDNLKQITQ LSDLEIATAS ISLSAFNDIQ RNHCELRSID ISRLLSKRAN RQELAYALQQ HANPGDLVVL PSIFGNGTGL SYLREIEQLT KLTLCEVPTM PPSLLGIRLE ESMKHAFIEL GGTMLNGDHV VQGEFSYVDK SDPEHSHYRL NRLFTKNHGD FPLQAKQFVL ATGSFFSQGL KANVDSMIEP IFGLDIAQSD KRTDWYSHDF FSTQSHPFLS MGIKTTANFQ AIKSGHVIDN LYCAGAILSG YNPILEGSGS GVAISSGFHA AESIIEQLQC SDSLQNNNTK AEVAL //