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Database: UniProt
Entry: A0A1M7MUQ1_9BACI
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ID   A0A1M7MUQ1_9BACI        Unreviewed;      1282 AA.
AC   A0A1M7MUQ1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Glucose/arabinose dehydrogenase, beta-propeller fold {ECO:0000313|EMBL:SHM94869.1};
GN   ORFNames=SAMN05216179_1380 {ECO:0000313|EMBL:SHM94869.1};
OS   Gracilibacillus kekensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=1027249 {ECO:0000313|EMBL:SHM94869.1, ECO:0000313|Proteomes:UP000184184};
RN   [1] {ECO:0000313|EMBL:SHM94869.1, ECO:0000313|Proteomes:UP000184184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10681 {ECO:0000313|EMBL:SHM94869.1,
RC   ECO:0000313|Proteomes:UP000184184};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FRCZ01000002; SHM94869.1; -; Genomic_DNA.
DR   RefSeq; WP_073201019.1; NZ_FRCZ01000002.1.
DR   STRING; 1027249.SAMN05216179_1380; -.
DR   OrthoDB; 9770043at2; -.
DR   Proteomes; UP000184184; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR012938; Glc/Sorbosone_DH.
DR   InterPro; IPR013783; Ig-like_fold.
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   InterPro; IPR029010; ThuA-like.
DR   PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF07995; GSDH; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF06283; ThuA; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184184};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..1282
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012771254"
FT   DOMAIN          702..783
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          894..1015
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          1031..1190
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          1049..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1282 AA;  142743 MW;  788B3ABD23D9CE55 CRC64;
     MVFKKKLSKI SLLIAMVLSL LIAPMLNPIA AFAHVGEHTG EEVHKLLVVT HTAGYRHGSI
     EDAKDVLPEW GEENNFEVTF VDETENARPD DLTLAEAFSD EFLADYDAIM FANTTSNFGT
     EAQREAVINF VENGGGFVGA HAAIDTGYDW PEYGEMVGTY FDSHPWTQEV NFLVEDDEHP
     STEHLTNGEW SKLEEVYIFP EDMNPREAGK HILLSLDTES VDGPRGGQFD DHPTSWCSPQ
     ESGRVFITAL GHHSQTWSSE EEFKQHILGG LDYAFGMETD TNCDQPSVKP GLISETLTDA
     VPRPTSLEVT DDNRVFSISI NGGVYETQPN GSTNEILEIN TTTEGEHGVM GIALDPEFED
     NGHIYIYYSV PGYTEDGEII NNLSRFTYED GSVSPSTEEV LLEVPSDPQC CHQAGFLEFG
     PDDKLYVTTG DNKPATNGPQ AESVETAQNL GDLRGSILRL NKDGSAPEDN PFVDVEGARD
     EIYAYGFRNP YRISFDPETG YIYEGDVGPD GDNDYDEFNV VTEPGQNFGW PYVIGDTPYD
     DYDQRFKDFA ANFDFSTVAG DFSADDVLTE PEEILDFAEN EAQDPIAFYP YGAKEPWGSG
     GRTSNAGPVY DPGSGENALP SSYDGKVLLY DFVRGWMKAV ETDENGEIVS VDDFIDGLML
     PMDVEVGPDG SIYVAEFGDS WWEVNEFSGI RKISWGVLER APNVQVKASA IYAQIGEEIT
     FDTTGTEDPD GDKISFEWDF GDGTTSSEES PSHTYTDNGE YTVRLTVTDH TGKSANWNQT
     ITIGNTPPTV EILEPADKTF FMNGDTFTFK GSAYDEEDGE IACENLEWRL DLLHDEHGHP
     QEYKTGCEVS YTLLDEGHNY NDNIWWQITL VANDNGNNGA PVLEGSQTIE FIKPRIEAEN
     FDDKSASIDT ETTSDIGGGQ NIGWTGEGEW LKYEGLNLER MEEIYLRTAS TMDYELEIRL
     DSPDGEAIAS IDGTATGDWQ QWNTISTELA EVSGTHDIYV YYVSGQTNIN WIQFAGPDFP
     PPTVDCGSNY CFEPITEFEN SIDRSNWTVD ASHNSESPDA GDAPSSLEYP LDNDLGTRWS
     SGENIQEGMY YQVNLGEMTV IDQIHVDSGS HWEERGLKDS HQDWFRGYKV EVSADGETWQ
     TVAEKEDNTE YIINAEFDAL PARYVKITNT QDNVEGDMWL AIHDLQVMAG ELDLVDTVDE
     LGNLLTEYIE SDDISNEQMA RALNTHLTSL NTFADNDQAE KVVKHLNTFI ALLDYQREQN
     AISELAHFDL KANAENLITL WQ
//
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