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Database: UniProt
Entry: A0A0K1E5U4_CHOCO
LinkDB: A0A0K1E5U4_CHOCO
Original site: A0A0K1E5U4_CHOCO 
ID   A0A0K1E5U4_CHOCO        Unreviewed;       515 AA.
AC   A0A0K1E5U4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Galactose oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CMC5_003600 {ECO:0000313|EMBL:AKT36246.1};
OS   Chondromyces crocatus.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC   Chondromyces.
OX   NCBI_TaxID=52 {ECO:0000313|EMBL:AKT36246.1, ECO:0000313|Proteomes:UP000067626};
RN   [1] {ECO:0000313|EMBL:AKT36246.1, ECO:0000313|Proteomes:UP000067626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm c5 {ECO:0000313|EMBL:AKT36246.1,
RC   ECO:0000313|Proteomes:UP000067626};
RA   Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT   "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT   high potential for natural compound synthesis and the genetic basis for the
RT   loss of fruiting body formation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012159; AKT36246.1; -; Genomic_DNA.
DR   RefSeq; WP_050428795.1; NZ_CP012159.1.
DR   AlphaFoldDB; A0A0K1E5U4; -.
DR   STRING; 52.CMC5_003600; -.
DR   KEGG; ccro:CMC5_003600; -.
DR   OrthoDB; 3420153at2; -.
DR   Proteomes; UP000067626; Chromosome.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   PANTHER; PTHR46093; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR46093:SF17; MULTIPLE EGF-LIKE-DOMAINS 8; 1.
DR   Pfam; PF13415; Kelch_3; 1.
DR   SMART; SM00612; Kelch; 4.
DR   SUPFAM; SSF117281; Kelch motif; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..515
FT                   /note="Galactose oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005458906"
FT   REGION          34..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  53100 MW;  484D9C7E47000A81 CRC64;
     MRTPNRSTTL VTLGLSAAAS SLVALAACSD SLHLDPQPTP PGSTSSGGQG GEGGGGAPCQ
     SNSDCTFPSS VCDPDRGECV ECLQHSDCSY APGTICSQGK CSCPEPGANF CPTLGAPNQA
     GYQASRCVDL SVSTADCGAC GHTCFGACND GACADPWEPT SLVGAPTARF AHVAVWTGSR
     MIVWGGQAVD AGNANSGGIY DPVMRTWTPT SLANAPSGRR NATAVWTGAR MLVWGGTNGS
     PLADGGIFDP VTNTWETLPA SGLGARMGHT AIWSGDRMIV WGGFDGANNR DDGAAFNPTT
     RSWAPLSGSN RPHRRHQHSA IWSDSQKKMV IFGGLGFDEL LNADDQYLNT LGAFSPSAGA
     DGTWEVGSTT NAPTARYGHT AVSAETYMLV WGGLGDLGLL NSGGRYDVVA AGWSAMHPEA
     PSPRYLHSAA WLGSARRMVI WGGHDGSTYL DNGGAYDNVN NRWHLDVSRG PSARGQHTAV
     VTDDDTMILW GGTGPSGSLN SGGILKPTAL GAGSN
//
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