ID GLPB_ENT38 Reviewed; 419 AA. AC A4WCP1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 16-JUN-2009, entry version 18. 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=Ent638_2806; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., RA Vangronsveld J., van der Lelie D., Richardson P.; RT "Complete sequence of chromosome of Enterobacter sp. 638."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000653; ABP61471.1; -; Genomic_DNA. DR RefSeq; YP_001177522.1; -. DR GeneID; 5110713; -. DR GenomeReviews; CP000653_GR; Ent638_2806. DR KEGG; ent:Ent638_2806; -. DR NMPDR; fig|399742.4.peg.2685; -. DR OMA; A4WCP1; TWLSQPF. 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 InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR Pfam; PF00890; FAD_binding_2; 1. DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1. DR PRINTS; PR00368; FADPNR. 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_1000062193. SQ SEQUENCE 419 AA; 45294 MW; 74EE67448AEB2560 CRC64; MKFDTVIIGG GLAGILCGLK LTQRGLRCAI VSRGQSALHF SSGSLDLLGA LPDGSAVDTP LMALQNPDAL PAEHPYRLVG TDNIARLADE TETLLATCGP RLRGHARQNH QRVTPLGMLR PAWLSPEEVP VAPIQSQRVC VVGISGFLDF QAHLAAASLR NQGISADTAE IELPELDVLR DNASEFRAVN IARFLDNDDK WPLLFDALQP LSQGCDALYM PACFGLADNR LWRWLSDRLA CALYLLPTLP PSVPGIRLHN QLQRQFIAQG GVWMAGDEVK KVTLDNGVVS ALWTRNHGDI PLRPRFVVLA SGSFFSNGLI STREGIREAV LGLDVRQNPS RADWYQSDFF APQPWQQFGV ITDNTLRPQL SGSPVDNLYA IGSVLGGFDP IALGCGGGVC AITALYAAEQ ICQRAGGEQ //