ID K2JS45_9PROT Unreviewed; 498 AA.
AC K2JS45;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:EKE78288.1};
GN ORFNames=P24_01966 {ECO:0000313|EMBL:EKE78288.1};
OS Oceanibaculum indicum P24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Oceanibaculaceae; Oceanibaculum.
OX NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE78288.1, ECO:0000313|Proteomes:UP000006746};
RN [1] {ECO:0000313|EMBL:EKE78288.1, ECO:0000313|Proteomes:UP000006746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P24 {ECO:0000313|EMBL:EKE78288.1,
RC ECO:0000313|Proteomes:UP000006746};
RX PubMed=23209207; DOI=10.1128/JB.01859-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL J. Bacteriol. 194:6942-6942(2012).
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|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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:EKE78288.1}.
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DR EMBL; AMRL01000002; EKE78288.1; -; Genomic_DNA.
DR RefSeq; WP_008943011.1; NZ_AMRL01000002.1.
DR AlphaFoldDB; K2JS45; -.
DR STRING; 1207063.P24_01966; -.
DR PATRIC; fig|1207063.3.peg.401; -.
DR eggNOG; COG0578; Bacteria.
DR Proteomes; UP000006746; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.250.1890; -; 1.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap 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; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000006746}.
FT DOMAIN 6..328
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 384..490
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 498 AA; 54648 MW; FDB9E7308D036FFC CRC64;
MSKIFDIAIV GGGVNGCGIA RDAAGRGLSV FLCEQQDLAG ATSSASTKLI HGGLRYLEYY
EFRLVREALI EREVLLGMAP HIAWPLRFVL PHHKGLRPAW LIRLGLFLYD HLGGRKILPG
TRTLDLSRDA AGAPLAGDFV KAFEYSDCWV EDSRLVVLNA MDAAARGTEI RTRTRCTGAR
RIDGVWEVTV EDAAGSRETV RAKSLVNAAG PWVSRFLTEG VGQNAAARIR MVKGSHIVVP
RLFDHDKAYI FQNSDGRIVF AIPYERDFTL IGTTDQDFRD DPAHVAISEE ETRYLCDAVS
GYLKQPVTPD MVVWTYAGVR PLYDDGASKA QAATRDYVLK LDAPEGAAPL LNIFGGKITT
YRKLAESALA LLKPHLPGMG KPWTEGATLP GGDFPVLGFA DQVAALRAAH PYLAEAHARR
LVRAYGTKAA ELLEGVTDTA GLGQHFGADL YEREVAYLMD REWAVSAADV LWRRSKLGLR
LTKEQAEALD GWMRNRPS
//