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Database: UniProt
Entry: A0A1Q4ZPW9_9ACTN
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Original site: A0A1Q4ZPW9_9ACTN 
ID   A0A1Q4ZPW9_9ACTN        Unreviewed;      1375 AA.
AC   A0A1Q4ZPW9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Galactose oxidase {ECO:0000313|EMBL:OKI48902.1};
GN   ORFNames=A6A27_36410 {ECO:0000313|EMBL:OKI48902.1};
OS   Micromonospora sp. CB01531.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI48902.1, ECO:0000313|Proteomes:UP000186700};
RN   [1] {ECO:0000313|EMBL:OKI48902.1, ECO:0000313|Proteomes:UP000186700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01531 {ECO:0000313|EMBL:OKI48902.1,
RC   ECO:0000313|Proteomes:UP000186700};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI48902.1}.
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DR   EMBL; LWLS01000113; OKI48902.1; -; Genomic_DNA.
DR   STRING; 1718947.A6A27_36410; -.
DR   Proteomes; UP000186700; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 4.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR46375:SF3; KELCH REPEAT AND BTB DOMAIN-CONTAINING PROTEIN 13; 1.
DR   PANTHER; PTHR46375; KELCH REPEAT AND BTB DOMAIN-CONTAINING PROTEIN 13-RELATED; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 2.
DR   Pfam; PF01344; Kelch_1; 2.
DR   SMART; SM00612; Kelch; 5.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 3.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186700};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          60..407
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
SQ   SEQUENCE   1375 AA;  141447 MW;  F005A981518E92F1 CRC64;
     MMMLSLASPA AASVNAGSSS TPMAAASGKS AAVRQCADPK PGHFVCMAMR RTDVTTHRGV
     QPQSAIPDGF GAGDLRSAYS LPADGGAGQI VAIVDAYDNP NAEADLAVYR QQYGLPPCTT
     ANGCFRKVDQ RGGMNYPPAD PGWAGEIALD LDMVSATAPY AHILLVEADT PSFEDMGAAV
     DEAVALGAKY VSNSYGTAYS ADPGTGEDPS EVTEADPHYN HPGVAIVASS GDSAFGVAYP
     AASQYVTAVG GTSLVRDSST RGWSESVWYN SGYGPGSGCS LYEAKPAWQT DSGCSKRTVA
     DVAAVADPAT GVAVYNSFQS GGWTVFGGTS ASAPIIAGVY AAAGTPVANT YPSSYPYANT
     GQLNDVSAGN NGTCSPAYLC TAGPGYDGPT GLGTPNGLAA FRTGPHGVVT GAVTNASTNA
     PVVGATVTVG VSTAITDVSG HYSATVPVGT YDATAAAYGY KSKTITGVGV TDGGSLTENF
     ALDPVPTSAV SGTVTDGSGH SWPLYATITV DGVPGGSVHT DPYTGRYSLQ LLQGQTYTLH
     VNANYPGYQA MTKDVTVGTS NVTAEFSVPV EVYDCLAPGY ATHNAGTTET FDATSIPARW
     TSDNTAGGGW AFDNPKLTAP YAPTDNVTGG SGGFAVTDTS TSSGPWDMSL ISPVTDLSDS
     GNPALSFNTD FRSFVSSADV DVTTDGGATW QNVWHKGYPE FRGPAWVDVP LPMVAHQSAV
     QVRFHYTSWA RTWWQIDNVF IGNRTCDPIP GGLVAGTVTD ANTNMPVVGV TVASGEKPAE
     HATSAGTPAD PKMADGFYSV FSSLTGTHDF TAERRYYATA TAHVNVVADA VTQTQFMLKA
     GKVMITPASV GITVPWQGKA GQAVTVQNTG SAPAKVTLGE QVGGVAPLTA HGAPTQRIQG
     TYSPLSLQDK DASIRQATGA APNGSVPAAA PWTTIADYPT TIQDNGVVSL GGRIYSAFGV
     TGSDYSHAMY AYDPTAGSWS RLASPADDRQ APVMAVLNGK IYATGGWGGW AVGGAPDGKT
     EVYDPATNVW TTAATNPNPL AGSAVAVLDG RMYVVGGCVL MECGTTDVMV YDPATDSWSH
     AADYPEPISW ESCGAISGAL YCAGGESKSR GTTRHTYGYD PHTDSWSPAA DMPIDLWGSG
     YTTAQGRLLL SGGVTEHSSV ITNQGFAFDP ASDTWTPIPN ANNALYRSGS ACGFYKIGGN
     TGGEDGGNLA SSEVLPGMVD CGETSRVSWL AVNPTTLTLA PGASATVTVA VDANVPDITQ
     PGTYTAAVVV GTDTPYAMPS VPVSMTVNQP KNWGKITGTV TGPSGPIRGA TVQITTPLGH
     YTLRTDASGH YQLWLDVRNN PLQVICAIDG YQPQAVTVKI KKGETTTLNF ALQKV
//
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