ID Q0I240_HISS1 Unreviewed; 562 AA.
AC Q0I240;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN Name=glpA {ECO:0000313|EMBL:ABI24789.1};
GN OrderedLocusNames=HS_0512 {ECO:0000313|EMBL:ABI24789.1};
OS Histophilus somni (strain 129Pt) (Haemophilus somnus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914 {ECO:0000313|EMBL:ABI24789.1};
RN [1] {ECO:0000313|EMBL:ABI24789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129PT {ECO:0000313|EMBL:ABI24789.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Dalin E., Tice H., Pitluck S., Brettin T.S., Bruce D., Challacombe J.F.,
RA Chertkov O., Detter J.C., Gilna P., Han S., Misra M., Tapia R.,
RA Thayer N.N., Xie G., Inzana T.J., Duncan A.J., Siddaramppa S.,
RA Richardson P.;
RT "Complete genome sequence of Haemophilus somnus 129PT.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000153,
CC ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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|ARBA:ARBA00005157}.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC GlpC. {ECO:0000256|ARBA:ARBA00011331}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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DR EMBL; CP000436; ABI24789.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0I240; -.
DR KEGG; hso:HS_0512; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_0_1_6; -.
DR UniPathway; UPA00618; UER00673.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) 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 CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR InterPro; IPR017752; G3P_DH_GlpA_su.
DR NCBIfam; TIGR03377; glycerol3P_GlpA; 1.
DR PANTHER; PTHR11985:SF36; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 18..367
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 441..492
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 562 AA; 61792 MW; 0269E80DC63B7468 CRC64;
MSMSSQKFSK DFPPLSADVI IIGGGATGAG IARDCALRGI DCILLERYDI ATGATGRNHG
LLHSGARYAV NDHESAEECI LENKILKRIA RHCVEDTKGL FITLPEDDLN YQKIFIQSCT
KAGIEAVPIE PDLARIMEPS VNPELIGAVV VPDGSIDPFR LTSANMLDAR EHGAKIFTYC
AVTQLIREGG RVIGTEVYDH KNKINRRFFA QVIVNAGGIW GQGIAEYADL KVKMFPAKGA
LLVMGHRINN LVINRCRKPA DADILVPGDT ICVIGTTSDR IPYDQIDNMI VTPEEVDILF
REGEKLAPSL RHTRVLRAYA GVRPLVASDD DPSGRNVSRG IVLLDHASRD GLEGFVTITG
GKLMTYRLMA EWATDLVSKK LGKQTVCTTA QELLPGSESD QNVPHINKII SLPTPLQISA
RYRHGQRASR LIGKERSDCT LVCECEAVTA GEVRYAVEEL KVNNLVDLRR RTRVGMGTCQ
AELCACRAAG LMARFHMATP RQSTLQLSSF MEERWRGIEP IAWGEAIREA EFSSWIYYSL
LGLNSVQSLT EQAQQGTDGN EI
//
