ID GLPB_ECOL5 Reviewed; 419 AA. AC Q0TFK1; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 24-MAR-2009, entry version 24. DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B; DE Short=Anaerobic G-3-P dehydrogenase subunit B; DE Short=Anaerobic G3Pdhase B; DE EC=1.1.5.3; GN Name=glpB; OrderedLocusNames=ECP_2284; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. CC Uses fumarate or nitrate as electron acceptor (By similarity). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone = CC glycerone phosphate + a quinol. CC -!- COFACTOR: FMN (By similarity). CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate CC (anaerobic route): step 1/1. CC -!- SUBUNIT: Composed of a catalytic glpA/B dimer and of membrane CC bound glpC (By similarity). CC -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B CC family. CC -!- SEQUENCE CAUTION: CC Sequence=ABG70278.1; Type=Erroneous termination; Positions=394; Note=Translated as Gly; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000247; ABG70278.1; ALT_SEQ; Genomic_DNA. DR RefSeq; YP_670179.1; -. DR GeneID; 4191933; -. DR GenomeReviews; CP000247_GR; ECP_2284. DR KEGG; ecp:ECP_2284; -. DR NMPDR; fig|340197.3.peg.306; -. DR HOGENOM; Q0TFK1; -. DR BioCyc; ECOL362663:ECP_2284-MON; -. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00753; -; 1. DR InterPro; IPR009158; Anaerobic_glycerol3P_DH_bsu. DR InterPro; IPR003953; FAD_bind2_N. DR Pfam; PF00890; FAD_binding_2; 1. DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1. DR TIGRFAMs; TIGR03378; glycerol3P_GlpB; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase. FT CHAIN 1 419 Anaerobic glycerol-3-phosphate FT dehydrogenase subunit B. FT /FTId=PRO_0000258901. SQ SEQUENCE 419 AA; 45393 MW; 8CC9C8ADE0ADB2E7 CRC64; MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH LPDGQPVTEI HSGLESLRQQ APAHPYTLLG PQRVLDLACQ AQALIAESGA QLQGSVELAH QRITPLGTLR STWLSSPEVP VWPLPAKKIC VVGISGLMDF QAHLAAASLR ELDLKVETAE IELPELDVLR NNATEFRAVN IARFLDNEEN WPLLLDALIP VANTCEMILM PACFGLANDK LWHWLNEKLP CSLMLLPTLP PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI PLRPRFAVLA SGSFFSGGLV AERDGIREPI LGLDVLQTAT RGEWYKGDFF APQPWQQFGV TTDEALRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC AVSALHAAQQ IAQRAGGQQ //