ID A0A0A8HQ95_STAHY Unreviewed; 557 AA.
AC A0A0A8HQ95;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=BUZ57_04070 {ECO:0000313|EMBL:RIO46670.1}, GLV83_07440
GN {ECO:0000313|EMBL:NJI31486.1};
OS Staphylococcus hyicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1284 {ECO:0000313|EMBL:RIO46670.1, ECO:0000313|Proteomes:UP000285625};
RN [1] {ECO:0000313|EMBL:RIO46670.1, ECO:0000313|Proteomes:UP000285625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 5959 {ECO:0000313|EMBL:RIO46670.1,
RC ECO:0000313|Proteomes:UP000285625};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:NJI31486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1380 {ECO:0000313|EMBL:NJI31486.1};
RA Rhoads D., Shwani A., Adkins P., Calcutt M., Middleton J.;
RT "Whole genome comparisons of Staphylococcus agnetis isolates from cattle
RT and chickens.";
RL Submitted (NOV-2019) 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|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 -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
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:RIO46670.1}.
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DR EMBL; WMFP01000035; NJI31486.1; -; Genomic_DNA.
DR EMBL; QXVO01000008; RIO46670.1; -; Genomic_DNA.
DR RefSeq; WP_039645962.1; NZ_WMFP01000035.1.
DR AlphaFoldDB; A0A0A8HQ95; -.
DR STRING; 1284.SHYC_07870; -.
DR GeneID; 41073356; -.
DR KEGG; shu:SHYC_07870; -.
DR HOGENOM; CLU_015740_5_2_9; -.
DR OMA; WAMAPHI; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000285625; Unassembled WGS sequence.
DR Proteomes; UP000606275; 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:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 22..378
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 407..532
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 557 AA; 62575 MW; 44188E5803EBFE40 CRC64;
MGRLSTLQRD SVKEKMQQEE YDLVIVGGGI TGAGVALDAS ARGMKVALLE MQDFASGTSS
RSTKLVHGGL RYLKQFQVGV VAETGREREI VYENGPHVTT PEWMLLPMHK GGTFGKFSTS
IGLAVYDRLA GVKKSERKRM LNVQETKDKE PLVKQDGLKG GGYYVEYRTD DARMTIEVMK
KAAEFGADII NYAKVSQFLY DNRNKVNGVR VIDRIKNEQF EIHGKKVVNA TGPWVDDVRS
NDYSKNNKEL RLTKGVHVVF DESKFPLHQA VYFDTEKDGR MIFAIPRDGK TYVGTTDTFY
NNDKASPLVN QEDRDYLINA INYMFPTVHV KDEDIESTWA GIRPLILEEG KDPSEISRKD
EIWEGDSGLL TIAGGKLTGY RHMANEIVDR VAKRLKQEYK LEFKPANTKN IPMSGGDVGG
SKNFESFVED KVKQAKGYNL DEKVARQLAK KYGSNVDELF ALTQAAQHQS TGLPLEMYVE
LLYGVQNELV VKPTDFLIRR TGALYFDIDS VQKYKDIVTN VLADLIGYDD NTKAVYKQEL
EDAITHAIHG QHQSATA
//