ID A9WJ20_CHLAA Unreviewed; 556 AA.
AC A9WJ20;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 OrderedLocusNames=Caur_3291 {ECO:0000313|EMBL:ABY36479.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY36479.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY36479.1; -; Genomic_DNA.
DR RefSeq; WP_012259132.1; NC_010175.1.
DR RefSeq; YP_001636868.1; NC_010175.1.
DR AlphaFoldDB; A9WJ20; -.
DR STRING; 324602.Caur_3291; -.
DR EnsemblBacteria; ABY36479; ABY36479; Caur_3291.
DR KEGG; cau:Caur_3291; -.
DR PATRIC; fig|324602.8.peg.3711; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_0_1_0; -.
DR InParanoid; A9WJ20; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000002008; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002008}.
FT DOMAIN 7..353
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 425..475
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 556 AA; 61010 MW; 697D55BF32004306 CRC64;
MQTISTDVLV IGGGATGTGC ALDLAMRGIR CVLVEKGDLT HGTTGRYHGL LHSGGRYVTK
DPQSASECAH ENAILRRIMP HCIEQTSGFF VITPWDDESY GDVFVANCHR TGVPVQEISV
AEMLRREPLL NPRISRVFEV PDGSADSFLA THSVALAARE YGADIRTYHH VVELIRVGDR
VVGAIAEDLR SGERVRIDCA YVLNAAGAWA GKIAALAGLT VNVVPGKGTM VAMNHRMVNT
VVNRCKLPSD GDIIVPIHTV AVIGTTDVHV PDPDVFGIEP EEIQFMLDEG EKLIPGFRQY
RALRAWAGVR PLYKDKDVAS DRDIPRTFKL LDHEERDGVS GIFSIVGGKW TTYRLMAEQT
VNEIARRLGN TQPCRTASEV LPVPRFEHSS RATVTVSPNP AAQTPHYWLG KPLALVESHH
AAGDLICECE LVTRDRIQAA IDAGAHNLDD IRRDVRMGMG PCQGGWCIYR TANLLYEQRC
AAGLSHVHTN EAIMHFLQER WKGLTPVLWG DQLRQARLDE LIYVGVLGID RLRTLAEPGG
GLVTQHPAIA TEYVQA
//
