ID Q1YEE0_AURMS Unreviewed; 467 AA.
AC Q1YEE0;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:EAS48651.1};
GN ORFNames=SI859A1_01135 {ECO:0000313|EMBL:EAS48651.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS48651.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS48651.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS48651.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:EAS48651.1}.
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DR EMBL; AAPJ01000008; EAS48651.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1YEE0; -.
DR HOGENOM; CLU_015740_5_0_5; -.
DR BioCyc; AURANTIMONAS:SI859A1_01135-MONOMER; -.
DR Proteomes; UP000000321; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000321}.
FT DOMAIN 3..305
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 350..454
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 467 AA; 51984 MW; 4A0F7153E7DFE193 CRC64;
MNDLASGTSS WSTKLVHGGL RYLEHYEFSL VRHALMEREV LWSIAPHIIR PLRFVLPHHD
GLRPAWLLRL GLFLYDHIGG RRKLKATTTV DLDGPLGAPL KDDFQKGFEY SDARVDDARL
VVLNARDAAA RGADIMVRTK VTEARRDKDG WVIALHDQET GAVRSVTARF LVNVGGPWVD
AIIQNAMGRN GANHIRLVQG SHIVTRKLYD HDRAYIFQNA DGRIIFTIPY EDDFTLVGTT
DQDYEGDPSQ VTISQSEIDY LLSAASEYFA KPVVAEDIVW TYSGVRPLFD DGASKAQEAT
RDYVLKVEGD NGEAPVLNCF GGKITTYRVL SEEVLGKIAH HLGAKGRSWT GDEPLPGGDF
AVDGVGALET ALRQAAPELD AATIHRLVRS YGTDAATFAR TGALGRDFGH GLYQAEIDWL
IAEEWARTAE DILWRRTKLG LRFRADETDA LAQYVTQRQN ERRTAAE
//
