ID G9ZAB4_9ENTR Unreviewed; 419 AA.
AC G9ZAB4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=HMPREF0880_04475 {ECO:0000313|EMBL:EHM44788.1};
OS Yokenella regensburgei ATCC 43003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Yokenella.
OX NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM44788.1, ECO:0000313|Proteomes:UP000003044};
RN [1] {ECO:0000313|EMBL:EHM44788.1, ECO:0000313|Proteomes:UP000003044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM44788.1,
RC ECO:0000313|Proteomes:UP000003044};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHM44788.1}.
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DR EMBL; AGCL01000047; EHM44788.1; -; Genomic_DNA.
DR RefSeq; WP_006820921.1; NZ_JH417874.1.
DR AlphaFoldDB; G9ZAB4; -.
DR STRING; 1002368.HMPREF0880_04475; -.
DR PATRIC; fig|1002368.3.peg.4082; -.
DR HOGENOM; CLU_047793_0_0_6; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000003044; 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}.
FT DOMAIN 4..399
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 419 AA; 45147 MW; 23E02738B0CD0EC0 CRC64;
MKFDTVIIGG GLAGLLCGLT LNQQGLRTAI VSRGQSALHF SSGSLDLLTA LPDGETVTDT
AAGLAELAIQ MPDHPYTRLG AEAVMQYAHA TEQLLAECGI EMHGSATRAH QRITPLGTTR
SAWLSPAEVP VMPLPGKRIG VIGISGFLDF QPHLAAASLS RHGMHTQTLE IDLPELDVLR
ENPTEFRAAN IARVLDDEAQ WPKLLAALQP LAENHDLLLM PACFGLQNAG LWQWLNAQLP
CPVCLLPTLP PSVPGMRLHA AMQRQFIRSG GTWLAGDEVV RVSHEEGNIS AIWTRNHGDI
PLRPRFAVLA SGSFFSNGLV ADRTGVREPI MGLDVAQLAS RRDWYQQDFF ASQPWQRFGL
VTDNQLRPSH QQVPFNNLFA IGSLIGGFDA IQLGCGGGVC AITAQHVARQ ILALAGGQS
//