ID A0A1F8SW67_9CHLR Unreviewed; 979 AA.
AC A0A1F8SW67;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN ORFNames=A2Z45_01740 {ECO:0000313|EMBL:OGO63851.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_55_16.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797669 {ECO:0000313|EMBL:OGO63851.1, ECO:0000313|Proteomes:UP000177674};
RN [1] {ECO:0000313|EMBL:OGO63851.1, ECO:0000313|Proteomes:UP000177674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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 -!- 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:OGO63851.1}.
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DR EMBL; MGOK01000106; OGO63851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SW67; -.
DR STRING; 1797669.A2Z45_01740; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000177674; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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:InterPro.
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; 4.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR003953; FAD-binding_2.
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 InterPro; IPR009158; G3P_DH_GlpB_su.
DR NCBIfam; TIGR03377; glycerol3P_GlpA; 1.
DR NCBIfam; TIGR03378; glycerol3P_GlpB; 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; PF00890; FAD_binding_2; 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; 2.
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 FMN {ECO:0000256|ARBA:ARBA00022643};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 8..353
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 408..460
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 565..955
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 979 AA; 107768 MW; 40E172C69CF634DB CRC64;
MRKIETEILV IGGGATGTGT IRDLAMRGYK AILVEKRDFS HGTTGRYHGL LHSGGRYVVK
DPLAAAECIA ENQILRRIMP HCIEDTGGYF VLTPWDDPNY VPAFLEGCWR AGIPVNEIAI
KQMLRAEPLL NTAILRCFHV PDAAADSFLA TEANVASARA YGAQVFNYLE VQELKRVGNR
VVGVRCYDLV KDEAVEIDAD LVVNAAGAWA GKIAGTAGIH IQIIPGKGTM VAINHRVLNT
VVNRCKMPAD GDIIVPIHTV AIIGTTDEPV ADPENLLIEP WEVSLMLEEG EKLIPGLKNM
RMLRAWAGVR PLYNETKPST TREISRAYVL LDHEERDGLS GLITITSGKW TTYRLMAEAT
VDLVGKKLGV QRSCRTHSEA LPGAEKGYYH HLGARLAQIE KDAAFNTLVC ECELATQADI
ITAIVDKEAK TLDDIRRDAR LGMGPCQGGF CTYRSAGILQ AIRHPPVEEI NLALRDFLQE
RWKGLLSILW GQQLRQERLD ELIYLNVLNV DHLPASRSSR LAAEVYAIPE GSGRIPGEPK
QRTKSEERMN EIEHLPSIAG QSHSDVLVIG AGLSGLVAAW QASARGRSTI LITQGWGATH
WHSGCIDVIG YLPNGNQEPV QSPIEALEIF LREHPDHPYS KTGLETLNEA IASFKWLCAD
NDYPLHGTLE HNWLLPSAVG AFRPSCLIPE TMIAGDLRRH DPMLIVGFDG FPDFYPGLIV
ENLKGQDIPA NEIVLDLPSL RNRRFVLPLI LARLFDTEEF RAEVIAALKP KLGECDRIGF
PAILGLERSK EARQDLEMRL NCPIFEIPTL PPSIPGIRLH NLLLKVIQKN GGTVYNGMQA
TAYESENSRI NGVWSEAASR RKYHPAKNFI LATGGILGGG ITGNPDGNVH EMVLNLPLTS
PIEHHDWFKP HFFDPLGHPI YQSGIPVNSM LQPLNNRGQV VFTNLFAAGT ALAGGDFLRE
RSLEGIALTT GFKVGEMIE
//
