ID A0A438MLA1_9ACTN Unreviewed; 1269 AA.
AC A0A438MLA1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glucose/arabinose dehydrogenase {ECO:0000313|EMBL:RVX46540.1};
GN ORFNames=EDD27_9430 {ECO:0000313|EMBL:RVX46540.1};
OS Nonomuraea polychroma.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX46540.1, ECO:0000313|Proteomes:UP000284824};
RN [1] {ECO:0000313|EMBL:RVX46540.1, ECO:0000313|Proteomes:UP000284824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX46540.1,
RC ECO:0000313|Proteomes:UP000284824};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RVX46540.1}.
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DR EMBL; SAUN01000001; RVX46540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438MLA1; -.
DR OrthoDB; 2479530at2; -.
DR Proteomes; UP000284824; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR PANTHER; PTHR19328:SF29; CALX-BETA DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR Pfam; PF07995; GSDH; 2.
DR Pfam; PF13385; Laminin_G_3; 2.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00282; LamG; 2.
DR SMART; SM00560; LamGL; 2.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000284824};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1269
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039608726"
FT DOMAIN 480..564
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 965..1061
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 222..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 132989 MW; D53B93FAA42184E0 CRC64;
MGGSVRRLLR CLVSAALLLA GLTALSSPAA ALPQRFHKQT IFSGLISPTN IEFAADGRVF
VAEKGGYIKV FDSLSDTTPT LYADLRTKVH DFWDRGLLGM ALHPNFPADP RVYVLYSYDA
EPGGTAPRWG QANEDYDECP SPPGPTGDGC RITGRLSVIS PSGAETPLIT DWCQQYPSHS
IGDLQFGRDG MLYASAGDGA SFEFPDYGQD NLTSSDIVPD NPCGDPPGAV GTALTPPSAE
GGTLRSQDLR TNGDPTGLDG TIIRINPDTG AAAPGNPNAG SSDPNTARVV AYGLRNPFRI
THRPGTDEIW SGEVGWGAYE ELNRIANPTG GVANFGWPCY EGPGLEDGYD ALNLTLCENL
YAAGPSAHQQ PYFSWNHDQR LYTGDPCAPG SQSSSSGVAF YNGGPYPDAY DGALFFSDYS
RRCVWVMSKG TNGLPDPATV SSFDTGIGTV ELETGPNGDL FAVDFDNGAI VRYIYDNSPP
TAVISATPTS GHAPLTVAFS GTGSSDADGD PLTYAWDLDG DGELDDSTSA TPSRTYTEIG
SYVVRLRVRD NQGGQGDATV TVNVGNSAPT AAISSPSSAT TWAVGDTIGF SGTGTDPEEG
AIPGSRMTWA LIMHHCPGAC HEHEITRYTG ASGSFQAPDH EHPSHLELRL IVTDEHGLTD
TKSVLLQPKT VNVTFQTNPP GLQLGFNQEQ TVTPFTRTVI VNSSNSITAP SPQSDYVFDA
WSDGGAATHN FAAPASATTY TATYKPAQTP AGLVAAYGMN EGAGTAVGDA SLYGNPGTTT
ATTWSASGKY GKALSFNGFS SWVTVNDAPS LRLTTGMTLE AWVRPTTVDS WRTVIMKQHT
GGLAYVLSAG SDTDRPHTVI HTAGEADIGG TASLPLNTWS HLAATYDGTT LRLHVNGTQV
SQRTAGGPIR TDNGALRIGG NSIWGEYFTG LIDEVRIYNR ALTALQIHTD MNTPIGEEPP
PDIQAPTAPG SLAAVGGAGN AQLTWSASTD NVGVEGYTVH RSTTPGFTPS GANQVGSSQT
TTFTDAGLAA GTYYYRVRAF DAASNLSPSS AEVSAAVTAP PANPGLVAAY GMNEGTGSTV
ADLSATGNTG TLTNTSWSAS GRHGSALAFN GSSSWVTVND APSLRLTTGM TLEAWVRPTT
VDSWRTVIMK QHTGGLAYVL SAGSDTDRPH TVIHTAGEAD IGGTASLPLN TWSHLAATYD
GTTLRLHVNG TQVSQRTAGG PIRTDNGALR IGGNSIWGEY FTGLIDEVRI YNRALTTTEI
QTDMNSPVS
//
