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
//