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GLPB_SHISS
ID   GLPB_SHISS              Reviewed;         419 AA.
AC   Q3YZW4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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}; OrderedLocusNames=SSON_2303;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000038; AAZ88948.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3YZW4; -.
DR   EnsemblBacteria; AAZ88948; AAZ88948; SSON_2303.
DR   KEGG; ssn:SSON_2303; -.
DR   HOGENOM; CLU_047793_0_0_6; -.
DR   OMA; CFGLENQ; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
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; -; 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   Pfam; PF00890; FAD_binding_2; 1.
DR   PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR03378; glycerol3P_GlpB; 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_0000258909"
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
 
 
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