GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0A8HQ95_STAHY
LinkDB: A0A0A8HQ95_STAHY
Original site: A0A0A8HQ95_STAHY 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system