ID Q1Z5A4_9GAMM Unreviewed; 442 AA.
AC Q1Z5A4;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 76.
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=P3TCK_17822 {ECO:0000313|EMBL:EAS43662.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS43662.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS43662.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS43662.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2006) 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:EAS43662.1}.
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DR EMBL; AAPH01000009; EAS43662.1; -; Genomic_DNA.
DR RefSeq; WP_006231474.1; NZ_CH724135.1.
DR AlphaFoldDB; Q1Z5A4; -.
DR HOGENOM; CLU_047793_0_0_6; -.
DR OrthoDB; 6395323at2; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000003789; 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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..412
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 442 AA; 48780 MW; D8EC61984CE549A2 CRC64;
MKFDSLIIGG GVAGLSCAIR CAEAGMKTAV IAAGQSALHF SSGSIDFLSR LPNGQPVYHP
MAAFDELQQQ NPEHPYCKLG KRKVQEALDW YQEMIKARGI YLSSQEDEAN HLRLTPMGTF
RSTWLSQQTV HQFPLTNTAG ELNHIALVTI DGFRDFQPKL AADNLSKLAQ FKDVKITTAA
VELPDFEEMQ RNPCEFRSID ISRVLRDERK LHAFAKSMIQ AVGKADLVVL PAVFGNGDGA
AVIKLLEGLT GFTICELPTM PPSLLGIRLE EAMKSHLKML GGIILVGDEV QRGDIEDGEL
KRIFTRNHRD MPLTADNYLI ATGSFFSRGM AAQRLNIDEP IFNLDTVAIP DRDQWYQPEF
FTSKAHPFLK MGVICNDQLQ ASANSQTIDN LFCAGALLAH YDPVFEGCGS GVAISTGFHV
AEQMISKHTA HQNQNNKERT VA
//
