ID A0A1N7C2Z0_9EURY Unreviewed; 556 AA.
AC A0A1N7C2Z0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN ORFNames=BB347_08825 {ECO:0000313|EMBL:APX96710.1}, SAMN05421809_1484
GN {ECO:0000313|EMBL:SIR57814.1};
OS Natronorubrum daqingense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=588898 {ECO:0000313|EMBL:SIR57814.1, ECO:0000313|Proteomes:UP000185687};
RN [1] {ECO:0000313|EMBL:APX96710.1, ECO:0000313|Proteomes:UP000187321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JX313 {ECO:0000313|EMBL:APX96710.1,
RC ECO:0000313|Proteomes:UP000187321};
RA Shuang W.;
RT "Complete genome sequence of Haloterrigena daqingensis type strain
RT (JX313T).";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SIR57814.1, ECO:0000313|Proteomes:UP000185687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8909 {ECO:0000313|EMBL:SIR57814.1,
RC ECO:0000313|Proteomes:UP000185687};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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 -!- 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}.
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DR EMBL; CP019327; APX96710.1; -; Genomic_DNA.
DR EMBL; FTNP01000002; SIR57814.1; -; Genomic_DNA.
DR RefSeq; WP_076580650.1; NZ_FTNP01000002.1.
DR AlphaFoldDB; A0A1N7C2Z0; -.
DR STRING; 588898.BB347_08825; -.
DR GeneID; 30956042; -.
DR KEGG; hda:BB347_08825; -.
DR OrthoDB; 36306at2157; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000185687; Unassembled WGS sequence.
DR Proteomes; UP000187321; Chromosome.
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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000185687}.
FT DOMAIN 7..363
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 437..487
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 556 AA; 60443 MW; 14EA83DE24B94612 CRC64;
MADDTEVLVL GGGSTGCGIA RDLAMRGLEV TLLERGTLTD GTTGRMHGLL HSGGRYAVSD
QASATECIEE NEILRDVASH CVEETSGLFV QRPEDPDEYF QEKLEGCRDC GIPARVLSGR
EAREVEPYLA DDVSRAIEVP DGAVDPFRLC VANALDAQNH GARIETHAEV IDLLREGDDI
YGVTVRHESG PGKRTHDTPG TTEEITAEYV VNATGAWAGQ IGAMADLDVA VRPSKGVMTI
MNVRQVDTVI NRCRPKGDAD IIVPHETTAI LGTTDEEVSD PDDYPEEQWE VDQMIDTLSE
LVPILEEART IRSFWGVRPL YEPPGTGTTD PTDITRDFFL LDHAERDGVS GMTSIVGGKF
TTYRAMAEEI SNHVCAKLGV SASCATAEEP LPGSENIEAL EAGMDQFGLR SPVARRSTQR
LGSRAQEVLE TNEANPVICQ CEGVTRAEVC DAIEQSGSDL NAVRIRTRAS MGNCQGGFCC
QNMANELHPT YDEATVRAAL DELFQERWKG ERHALWGEQL SQAMLNYALH ATTMNRDQDP
ADASTGFDYA RFDGGA
//
