ID A0A2T5BYG8_9BACT Unreviewed; 1281 AA.
AC A0A2T5BYG8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Alpha-glucosidase (Family GH31 glycosyl hydrolase) {ECO:0000313|EMBL:PTN07288.1};
GN ORFNames=C8N47_1191 {ECO:0000313|EMBL:PTN07288.1};
OS Mangrovibacterium marinum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mangrovibacterium.
OX NCBI_TaxID=1639118 {ECO:0000313|EMBL:PTN07288.1, ECO:0000313|Proteomes:UP000243525};
RN [1] {ECO:0000313|EMBL:PTN07288.1, ECO:0000313|Proteomes:UP000243525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28823 {ECO:0000313|EMBL:PTN07288.1,
RC ECO:0000313|Proteomes:UP000243525};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
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:PTN07288.1}.
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DR EMBL; QAAD01000019; PTN07288.1; -; Genomic_DNA.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000243525; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14254; Dockerin_II; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd06596; GH31_CPE1046; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PTN07288.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243525};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1281
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015662206"
FT DOMAIN 862..943
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1084..1153
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
SQ SEQUENCE 1281 AA; 142620 MW; 4840882CCF983FC5 CRC64;
MKRVVLKSGA FLAFAWLFFS SSLAFAQDET TAKTGSGQEQ IEVLTARKTN STTVEIEFSN
QQKMVIDFYG DNIFRMFQDP RGKGLRAPQA EPPAEILVQN PRKAVLELQL KDAGNTVSIQ
SSAVLLTFDK TNATFELKNT TTGKTVVRSL APIAFGKDKV ELQLSEQPNE YFYGGGVQNG
RFSHKGKVIA IENQNSWTDG GVASPTPFFW STNGYGFMAY TFAKGNYNFG AKGENRVALS
HDTGYLDVFF MVSDGAVALL NDFYQLTGQP VLIPKFGFYE GHLNAYNRDY WKEDSAGILF
EDGKRYRESQ KENGGIKESL NGEKNNYQFS ARAVVDRYAE HDMPLGWILP NDGYGAGYGQ
TSTLDGNIAN LKEFGDYARG HGVEIGLWTQ SDLHPIDTVE ALLQRDIVKE VGVAGVRVLK
TDVAWVGAGY SFGLNGVQDA AEIMQKEGNQ ARPFIISLDG WAGTQRYATI WSGDQTGGKW
EYIRFHIPTF IGSGLSGQPN ITNDMDGIFG GKNSIVNIRD FQWKTFTLMQ LNMDGWGANE
KYPQALGEPA TSINRNYLKL KSELLPYAYT VAREAVDGMP AIRAMFLEEE NPYTLGKNTQ
YQFMFGPDFL VAPIYQNTKS DSEGNDIRNQ IYLPEGNWVD YFTGEIYAGG RIINNFEAPI
WKLPVFVKMG AIIPMVDPNN NVNEIDRQRR IYEFYPSGQS SFVEYDDDGL TTAYQQGQYT
KTRIGSVLNG DQLSLVVEPA KGTFAGFVNE KETELRINLS REPGKIAATI GDKKVKLKRV
NSLADFKAGT NVYYYNAAPD MNRFATAGSE FEQVKMIRNP QLMVKIEKTD ISQNRISLQF
KGYAFESEDR LLKSTGELTE VKNAAVSASN ATAYSLTPSW DKIANADCYE IQFQGMLYAN
ITDNELLFEN LEPETTYEFS IRAVNKSGHS DWTHFTAKTK ADPLQFALKG LTAVSSAKMQ
GGQGLNRLFD FDENSMMHTD YAGNSVPFDM VIDLKSVSQL EKIVYLPRMS GRNGIIQSGA
FQYSKDKENW TDAGRFEWKA DNQPKTFELK DQPVARYLKM EVDKAYGDFG SGRQLYIFKV
PGTESFLPGD INSDGVIDSN DLTSYLNYTG LRKDDSDFGY VSRGDVNENG LIDAYDISNV
ATQLDGGVSS QNEGTLAGEL HLNASKRSYK AGEIVELKVE GRQLEAVNAF SCAIPYSPSD
LEYVGVKTMN TKGMDNMTYN RLHSNGDRVL YPTFVNVGGQ PALRGDGTIL TIQFKAKRAF
TFGLELQNGL LIDKQLNTVN F
//
