ID R4W8S7_9EURY Unreviewed; 599 AA.
AC R4W8S7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=L593_10540 {ECO:0000313|EMBL:AGN02053.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN02053.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN02053.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN02053.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP005962; AGN02053.1; -; Genomic_DNA.
DR AlphaFoldDB; R4W8S7; -.
DR STRING; 1333523.L593_10540; -.
DR KEGG; sali:L593_10540; -.
DR PATRIC; fig|1333523.5.peg.2173; -.
DR eggNOG; arCOG05746; Archaea.
DR HOGENOM; CLU_015740_0_1_2; -.
DR OrthoDB; 36306at2157; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000014072; 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; 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; 3.30.9.10; 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; 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:UP000014072}.
FT DOMAIN 8..369
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 444..491
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT REGION 545..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 64962 MW; D331A3ACDECD2A96 CRC64;
MIESTTGVLV IGGGSTGTGV ARDLAMRGLD VTLVEKGNLT HGTTGRMHGL LHSGGRYAVS
DQPSAVECIE ENRVLRDIAS HCVEETGGLF VKRPEDGEDY FQQKLEGCRE CDIPAEVLSG
EEAREVEPYL AKDIDKAIWV PDGAIDPFRL CVANAESATD HGARIQTHAE VTDVLIDEPE
GTDERRVVGV EVRQTGGTGT RTHGVAEETE RIYADHVVNA TGAWAGQLGE MAGVEVAVQP
SKGAMTVMNV RQVDTVVNHC RPKGDADIVV PHETTAILGT TDEAVDDPEH YPEEQWEVDL
LIDNLAELVP ILSEARTIRT FWGVRPLYEP PGTGTQDTTD ITRDFFLLDH GERDDLPGMT
SIVGGKFTTY RMMAEQISDH VCDLLGVSAE CRTADVPLPG SEKPGRLDDA MEQYGLRSPI
ARRSAERLGS RTEAVLGTDA PNPVVCECEG VTRAELQHAI EGAGSDLNDV RIRTRASMGN
CQGGICAHRM AAELHPRYEA NAIRESHDEL LQERWKGERH ALWGDQLAQA ALNYALHATT
MNLDRDPART GETPDFEAFD GGPTQTVAQP AADGGRRTGR GGDPPTDGDR DDRRRDDGD
//
