ID   U2QAM5_LEPWF            Unreviewed;      1018 AA.
AC   U2QAM5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Alpha amylase, catalytic domain protein {ECO:0000313|EMBL:ERK53441.1};
GN   ORFNames=HMPREF9015_00521 {ECO:0000313|EMBL:ERK53441.1};
OS   Leptotrichia wadei (strain F0279).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=888055 {ECO:0000313|EMBL:ERK53441.1, ECO:0000313|Proteomes:UP000016626};
RN   [1] {ECO:0000313|EMBL:ERK53441.1, ECO:0000313|Proteomes:UP000016626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0279 {ECO:0000313|EMBL:ERK53441.1,
RC   ECO:0000313|Proteomes:UP000016626};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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:ERK53441.1}.
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DR   EMBL; AWVM01000026; ERK53441.1; -; Genomic_DNA.
DR   RefSeq; WP_021746004.1; NZ_KI271395.1.
DR   AlphaFoldDB; U2QAM5; -.
DR   PATRIC; fig|888055.3.peg.500; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_296620_0_0_0; -.
DR   Proteomes; UP000016626; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11338; AmyAc_CMD; 1.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   CDD; cd02857; E_set_CDase_PDE_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF210; MALTODEXTRIN GLUCOSIDASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          339..918
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1018 AA;  119737 MW;  3685BDF9C3F6E90B CRC64;
     MGYKLIIYKD NKFYREENLK QKWENFIYKW GNVESGSYFF EIKDEENGTI SGVTYSHTAP
     FAKKFEAVVG ENLPPKSITG FQKGIDIYVE YSPSKKSFSL TKMKFYRMNL NIADFGLEKA
     DKVEIAGNFN NWKPDTEPIH HFEGTNYEVT LASPEGVYEY KYLIDGKWYP GNENKKLIIG
     ENGALFAQGD LGTGKFVYEA IDKNTNLKAI VHNYDSLQYF NKLSDSEYEF KIRTQMNDVE
     RAYISIVLHE EDNYEMIYEL ERYQDKTNGF DYFERIINFG KEATKLLYYF ILEDNGSRAY
     FNGKTLSYSK PKRLVVNTTS KDIQLFNVPN WAKEAIWYNI FPDRFYNGNH YNDPIFNEFG
     PEAFKPNRLH EQNFVEEYKW EKSNNVISHF DRNRWTADFK EQVIWEKLGE REIDYSLKYA
     RMYGGDLQGI KEKIPYMKEL GINAVWLNPV FFSYQNHKYG ANDFRHISPD FGTIKTSGST
     HGVEINRNNK YGNKSYVDVL GNKATTSSEL KLLEVNLKGE NRGKNGYGET EDPATWVWTE
     SDLIMVDLIK EFHKNGIRVI FDGVFNHSSS EHWTFNMVLA DGENSKYKDW YKFTDFGQHV
     PITDDMSDEQ AFETLIANRK RTIYNAWGGF DSLPEFNTFN QEYKEYIFNI TRKWMCGPDG
     KESENWMEDD GIDGWRLDVP NCLENQNFWN EWREVVKGSK KDSYITAELW GNASGDINGG
     NKFDTVMNYE WLKTVIGFFI NQSREGGVRY KLKAQDFFNE LREKRTWYPY QALQASQNLN
     GSHDTDRLYS RIVNDVIGRN LEEGKQLEKG YNGIRPDLAS NYHPNTTIDW RNSPIKPKDI
     LKLISIFQMT YIGAPMLFYG DEVGMWGATD PYCRKPMLWK EFLYDNEKNP SHINQNEVYE
     QKVDSDLFEW YKKLIRIRLE NKTLVYGKFR EIFADNDREI IVYERVIEDH TIIVVINNSF
     NNWENVEFET NYQDERFIDL VTEGRTFRTG SNGKLKLDLK AKEGMILRKK VRIDGDYE
//