ID X5M4M1_BARHN Unreviewed; 510 AA.
AC X5M4M1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:CDO46896.1};
GN ORFNames=BM1374165_00888 {ECO:0000313|EMBL:CDO46896.1};
OS Bartonella henselae (Rochalimaea henselae).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=38323 {ECO:0000313|EMBL:CDO46896.1, ECO:0000313|Proteomes:UP000019801};
RN [1] {ECO:0000313|Proteomes:UP000019801}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BM1374165 {ECO:0000313|Proteomes:UP000019801};
RA Raoult D.;
RT "Genome sequencing of Bartonella spp. isolated from human blood.";
RL Submitted (NOV-2013) 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|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}.
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DR EMBL; HG969191; CDO46896.1; -; Genomic_DNA.
DR RefSeq; WP_038487593.1; NZ_LOAH01000012.1.
DR AlphaFoldDB; X5M4M1; -.
DR STRING; 38323.BM1374165_00888; -.
DR KEGG; bhs:BM1374165_00888; -.
DR PATRIC; fig|38323.4.peg.952; -.
DR Proteomes; UP000019801; Chromosome.
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}.
FT DOMAIN 14..341
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 394..500
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 510 AA; 58322 MW; 688945140E934B60 CRC64;
MMKSEIMETA THYDLFIIGG GINGCGLARD AAGRGFKVGL AEMNDLASGT SSASTKLIHG
GLRYLEYYEF RLVREALKER EIIWRMAPHI VRPLRFLLPY HKKLRPAWML RFGLFIYDYL
GNWNQKLWRS KTVNFSKSFC SILKEEYHKG FEYSDARVDD ARLVIANARD AEKWGAVIKV
RTEVLSLKSE EKKWVVILRD KLSGKESCVT ASYVANMTGP WINHILSNVL DCKENPPVRL
VRGSHILVPK LYAHDRAYIF QNGDGRILFS IPYQEEFTLL GTTDCDYQGD PADVHITDTE
IDYICTAASE YFVQPVLRES IVWTYSGVRP LYDDGASKAQ EITRDYVLKE MGTESTPRIL
NLYGGKITTY RKLAEDAMKF VEKALGKKGK PWTINSTLPG GDFPHNKLDT IENKIALLVP
DLDAFTYRRL ARSYGCEALM IFANGKADKG KNFGHGLYEV EVKWLMEKEW AKTCEDVLWR
RSKLGLLFNK KEIDALTAYM QKIKDNEQNS
//
