ID X7FA18_9RHOB Unreviewed; 534 AA.
AC X7FA18;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=RISW2_22435 {ECO:0000313|EMBL:ETX29645.1};
OS Roseivivax isoporae LMG 25204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX29645.1, ECO:0000313|Proteomes:UP000023430};
RN [1] {ECO:0000313|EMBL:ETX29645.1, ECO:0000313|Proteomes:UP000023430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX29645.1,
RC ECO:0000313|Proteomes:UP000023430};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL Submitted (JAN-2014) 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}.
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:ETX29645.1}.
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DR EMBL; JAME01000008; ETX29645.1; -; Genomic_DNA.
DR RefSeq; WP_043768439.1; NZ_JAME01000008.1.
DR AlphaFoldDB; X7FA18; -.
DR STRING; 1449351.RISW2_22435; -.
DR PATRIC; fig|1449351.3.peg.1427; -.
DR eggNOG; COG0578; Bacteria.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000023430; 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; 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:UP000023430}.
FT DOMAIN 12..389
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 412..513
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 534 AA; 60132 MW; 390C7FE83CF20F8F CRC64;
MADRTEPPGT YDLFIIGGGI NGCGIARDAA GRGLNVGLAE MNDLASATSS ASTKLFHGGL
RYLEYFEFRL VRESLIERET LMRAMPHISW PMRFVLPFHR DMRFESSTPT SKLLNTVMPW
MKGRRPSWLI RLGLFLYDNL GGREILPGTR TLDLTRAPEG RPLKERFRHA YEYSDCWVQD
SRLVVLNARD AEARGADILT RTRVTVAERD GDHWRIGLAD RETGATRTVT ARMLVNAGGP
WAGEIIRGVV RSNATDTVRL VRGSHIVCRK LYEHDKCYFF QGTDGRIVFA IPYEQDFTLI
GTTDSEQDDP DRRPECTPEE RDYLIAFANA YFREELTADD VVWSYSGVRP LYDDGASSAT
AATRDYTLKV DDAGGAPLLN IFGGKITTYR RLAESALDRI APFFPGLKGK WTAGVTLPGG
DFKVVETRGK IEDLAEAYPF LGHRWAERMI RHYGTESWTI LGDAREAADL GRDFGHTLTE
AEVRWLMTRE YARTAEDVLF RRTRLGIRAT EAQIADLDGW MQDARAEHGA HAAQ
//
