(data stored in SCRATCH zone)

SWISSPROT: C3MGS4_SINFN

ID   C3MGS4_SINFN            Unreviewed;       403 AA.
AC   C3MGS4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   SubName: Full=Glycolate oxidase, subunit GlcE {ECO:0000313|EMBL:ACP24189.1};
DE            EC=1.1.3.15 {ECO:0000313|EMBL:ACP24189.1};
GN   Name=glcE2 {ECO:0000313|EMBL:ACP24189.1};
GN   OrderedLocusNames=NGR_c03930 {ECO:0000313|EMBL:ACP24189.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24189.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24189.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR   EMBL; CP001389; ACP24189.1; -; Genomic_DNA.
DR   RefSeq; WP_012706974.1; NC_012587.1.
DR   RefSeq; YP_002824942.1; NC_012587.1.
DR   STRING; 394.NGR_c03930; -.
DR   EnsemblBacteria; ACP24189; ACP24189; NGR_c03930.
DR   GeneID; 7791619; -.
DR   KEGG; rhi:NGR_c03930; -.
DR   PATRIC; fig|394.7.peg.3199; -.
DR   eggNOG; ENOG4105EU8; Bacteria.
DR   eggNOG; COG0277; LUCA.
DR   HOGENOM; HOG000230994; -.
DR   KO; K11472; -.
DR   OMA; WGTLAVM; -.
DR   OrthoDB; POG091H0N9H; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; C3MGS4.
DR   SWISS-2DPAGE; C3MGS4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Oxidoreductase {ECO:0000313|EMBL:ACP24189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        1    182       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   403 AA;  41958 MW;  6DA64399B5734222 CRC64;
     MIVHFEPASE EGIASVVRSA AAERVTLAIV GGGTRSGLGN PVRADRTLST RRLAGIVAYH
     PAEMTMSALA GTPLAEVEAA LAANGQMLSF EPMDHRPIFG TTGEPTIGGV FAANVSGPRR
     YVAGAARDNL LGVRFVNGRG ELIKAGGRVM KNVTGLDLVK LMAGSYGTLG ILTEVTFKVL
     PVPPAAATVV VSGLNDAEAA AVMAEAMAQP VEVSGAAHLP ESVRGRFIDG ALPEGAATVL
     RLEGLAASVE MRAEKLVAAL SRFGSRSQLD AGQAKALWAE IRNVKPYADG TARPLWRVSV
     APSAGHQLVA ALRLQTGVDA FYDWQGGLVW LRMEAEAEAE LVRRYVGALG GGHATLVRAD
     GEARARAPAF EPQAPAVAQL SERVRATLDP ARIFNPGRLA AVA
//

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