ID GLPB_ECO8A Reviewed; 419 AA. AC B7M5S7; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 77. 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=ECIAI1_2320; OS Escherichia coli O8 (strain IAI1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585034; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IAI1; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). 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; CU928160; CAQ99164.1; -; Genomic_DNA. DR RefSeq; WP_001209921.1; NC_011741.1. DR AlphaFoldDB; B7M5S7; -. DR GeneID; 75205705; -. DR KEGG; ecr:ECIAI1_2320; -. DR HOGENOM; CLU_047793_0_0_6; -. DR UniPathway; UPA00618; UER00673. 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 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..419 FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit FT B" FT /id="PRO_1000133358" SQ SEQUENCE 419 AA; 45415 MW; 681241440AE851D9 CRC64; MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQPVTDI HSGLESLRQQ APAHPYSLLE PQRVLDLACQ AQALIAESGA QLQGSVELAH QRVTPLGTLR ATWLSSPEVP VWPLPAKKIC VVGISGLMDF QAHLAAASLR ELDLSVETAE IELPELDVLR NNATEFRAVN IARFLDNEEN WPLLLDALIP VANTCEMILM PACFGLADDK LWRWLNEKLP CSLMLLPTLP PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI PLRPRFAVLA SGSFFSGGLV AERNGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV TTDETLRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ //