(data stored in SCRATCH zone)

SWISSPROT: C3MGS3_SINFN

ID   C3MGS3_SINFN            Unreviewed;       479 AA.
AC   C3MGS3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:ACP24188.1};
DE            EC=1.1.3.15 {ECO:0000313|EMBL:ACP24188.1};
GN   Name=glcD2 {ECO:0000313|EMBL:ACP24188.1};
GN   OrderedLocusNames=NGR_c03920 {ECO:0000313|EMBL:ACP24188.1};
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:ACP24188.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24188.1, 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; ACP24188.1; -; Genomic_DNA.
DR   RefSeq; WP_012706973.1; NC_012587.1.
DR   RefSeq; YP_002824941.1; NC_012587.1.
DR   STRING; 394.NGR_c03920; -.
DR   EnsemblBacteria; ACP24188; ACP24188; NGR_c03920.
DR   GeneID; 7791618; -.
DR   KEGG; rhi:NGR_c03920; -.
DR   PATRIC; fig|394.7.peg.3198; -.
DR   eggNOG; ENOG4105CQB; Bacteria.
DR   eggNOG; COG0277; LUCA.
DR   HOGENOM; HOG000230998; -.
DR   KO; K00104; -.
DR   OMA; RDLMRHQ; -.
DR   OrthoDB; POG091H02HQ; -.
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; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
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; C3MGS3.
DR   SWISS-2DPAGE; C3MGS3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Oxidoreductase {ECO:0000313|EMBL:ACP24188.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN       52    230       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   479 AA;  50781 MW;  69FBD4AE2F8DB3B6 CRC64;
     MPETIGFLKP RQAVLDRRPE IIADLADLLP EGCLISDERG LKPFETDAFL AYRRLPLAVV
     LPETTEQVSA VLKYCSRYGI PVVPRGAGTS LSGGAIPQED AIVIGLSKMS RILDVDLFNR
     TATVQAGVTN LNISDAVSAD GFFYAPDPSS QLACTIGGNI GMNSGGAHCL KYGVTTNNLL
     GVKMVLFDGT VIELGGKALD SSGYDLLGLV CGSEGQLGIV TEATVRLIAK PEGARPVLFG
     FASSVAAGSC VADIIGSGII PVAIEFMDKP AIEICEAFAH AGYPLDVEAL LIVEVEGSEA
     EMDTMLESII AIARRHGVMT IKESQSALEA ALIWKGRKSA FGATGRVADY ICMDGTVPLS
     QLSHVLRRTG EIVASYGLRV ANVFHAGDGN MHPLILYNIN DPEDAARAEA AGNDILKLCV
     DAGGCLTGEH GVGIEKRDLM RHQYNKADLD QQMAVRAAFD PQWLLNPSKV FPLEGRPAA
//

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