ID R8ASJ9_PLESH Unreviewed; 427 AA.
AC R8ASJ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B {ECO:0000256|HAMAP-Rule:MF_00753};
DE Short=Anaerobic G-3-P dehydrogenase subunit B {ECO:0000256|HAMAP-Rule:MF_00753};
DE Short=Anaerobic G3Pdhase B {ECO:0000256|HAMAP-Rule:MF_00753};
DE EC=1.1.5.3 {ECO:0000256|HAMAP-Rule:MF_00753};
GN Name=glpB {ECO:0000256|HAMAP-Rule:MF_00753};
GN ORFNames=PLESHI_06107 {ECO:0000313|EMBL:EON89293.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89293.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON89293.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON89293.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC fumarate or nitrate as electron acceptor. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00753};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00753}.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC GlpC. {ECO:0000256|HAMAP-Rule:MF_00753}.
CC -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC family. {ECO:0000256|HAMAP-Rule:MF_00753}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EON89293.1}.
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DR EMBL; AQQO01000038; EON89293.1; -; Genomic_DNA.
DR RefSeq; WP_010862846.1; NZ_KB944507.1.
DR AlphaFoldDB; R8ASJ9; -.
DR STRING; 703.SAMEA2665130_00153; -.
DR PATRIC; fig|1315976.3.peg.1202; -.
DR HOGENOM; CLU_047793_0_0_6; -.
DR OrthoDB; 6395323at2; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000014012; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00753};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00753};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00753}; Reference proteome {ECO:0000313|Proteomes:UP000014012}.
FT DOMAIN 4..407
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 427 AA; 46403 MW; C98FB224E4CFB38C CRC64;
MKFDVAIIGA GLAGLTCGIQ LAASGQRCTI ISAGQCALNF SSGSLDLLSR LPDGTAVAAP
LQALDQLTTQ APQHPYTRMG SAAMTRHVAH FMQLLQASNI EMQGEAQYNH LRMTPLGSLR
PTWLSPLSVP VQPLPLPAQS GALALIGIEG FHDFQPEMAA ATLQQYPAYQ GCQILTGQLT
LPQLDQLRRN PSEFRSVNVA RVLEQLTDLA PLAAELKRAA QSATTVILPA VLGLENTRLR
SELERLTGLQ LLELPTLPPS VLGIRLQQAL KRRFQQLGGL FMNGDQVQSA RIENQRVTAL
YTRNHEEIPV EARDVVLASG SFFSNGLVAE FDRIREPVFG LDVIETGPRA EWSEERFLTS
QPFLQFGVSV DNRLRVRKDG QTLHNVYAIG AVLGGYDPIY QGCGAGVSVT TALHVAEQIL
QQQEETA
//
