UniProt: A0A0U3HRU6

Database: UniProt
Entry: A0A0U3HRU6_9MICC

LinkDB:  A0A0U3HRU6_9MICC 
Original site:  A0A0U3HRU6_9MICC

All links

Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (9)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
All databases (17)   

Download RDF

ID   A0A0U3HRU6_9MICC        Unreviewed;       582 AA.
AC   A0A0U3HRU6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=AS188_11245 {ECO:0000313|EMBL:ALU40230.1}, KFL01_16390
GN   {ECO:0000313|EMBL:GEO92333.1};
OS   Kocuria flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU40230.1, ECO:0000313|Proteomes:UP000057181};
RN   [1] {ECO:0000313|EMBL:ALU40230.1, ECO:0000313|Proteomes:UP000057181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO-9041 {ECO:0000313|EMBL:ALU40230.1,
RC   ECO:0000313|Proteomes:UP000057181};
RA   Zhou M., Dai J.;
RT   "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GEO92333.1, ECO:0000313|Proteomes:UP000321155}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO92333.1,
RC   ECO:0000313|Proteomes:UP000321155};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL   Submitted (JUL-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|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   ---------------------------------------------------------------------------
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; CP013254; ALU40230.1; -; Genomic_DNA.
DR   EMBL; BJZR01000039; GEO92333.1; -; Genomic_DNA.
DR   RefSeq; WP_058858931.1; NZ_CP013254.1.
DR   AlphaFoldDB; A0A0U3HRU6; -.
DR   STRING; 446860.AS188_11245; -.
DR   KEGG; kfv:AS188_11245; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000057181; Chromosome.
DR   Proteomes; UP000321155; 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:UP000057181}.
FT   DOMAIN          25..390
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          412..537
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   582 AA;  62688 MW;  C1B73B1BDE372148 CRC64;
     MAHPTLSATD RARALDAMSG GPELDVLVVG GGITGAGIAL DAATRGLRTG IVEAQDWAGG
     TSQWSSKLVH GGLRYLQQLD FKLVAEALRE RELLLDFLAP HLVKPVPFLY PLTHRWWERP
     YVAAGIGLYD ALAHLGAKVA TLPYQRHLTA AGVARVFPDV KPGSMVGAVQ YWDARVDDAR
     LVLTIVRTAV RHGALAANRA RAVDFPRDAG GRVTGAVVRD LETGRERTVR ARTVIAATGV
     WTERIQDRAQ AEGGLKVLAS KGIHIVVPRE RIRSDTGLIL QTEKSVLFII PWERYWLIGT
     TDTPYEQELE NPVATSADID YVLEHANVVL DEPLGRGDVI GVYAGLRPLL QPGTKGGGEP
     AQSTKISREH TVTEVVPGLI TIAGGKLTTY RVMAEDAVDL ALGAGRAKEL PSVTDRTALL
     GADGYLALRR RAGTLGSAHG WDEEQVLHLL RRYGSAVEEI LELVEQRPDL GRPLGGAAPY
     LRAEIVHACT HEGALHLEDV FDTRTRLTWE RPRHGLDALD EIAELAAGAL GWDADRRAAE
     VEAYRLRCAA EDAAAAAPDD AAAAAARAAA PDVLELVRRD AG
//

DBGET integrated database retrieval system