ID D1AGK8_SEBTE Unreviewed; 1012 AA.
AC D1AGK8;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Alpha amylase catalytic region {ECO:0000313|EMBL:ACZ10960.1};
GN OrderedLocusNames=Sterm_4128 {ECO:0000313|EMBL:ACZ10960.1};
OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Sebaldella.
OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ10960.1, ECO:0000313|Proteomes:UP000000845};
RN [1] {ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA Woyke T., Wu D., Eisen J.A.;
RT "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ10960.1, ECO:0000313|Proteomes:UP000000845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX PubMed=21304705;
RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Chen F.;
RT "Complete genome sequence of Sebaldella termitidis type strain (NCTC
RT 11300).";
RL Stand. Genomic Sci. 2:220-227(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; CP001739; ACZ10960.1; -; Genomic_DNA.
DR RefSeq; WP_012863535.1; NC_013517.1.
DR AlphaFoldDB; D1AGK8; -.
DR STRING; 526218.Sterm_4128; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; str:Sterm_4128; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_296620_0_0_0; -.
DR Proteomes; UP000000845; Chromosome.
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 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 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000000845}.
FT DOMAIN 338..917
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1012 AA; 119628 MW; F0A2797E04801FA8 CRC64;
MIYKLIIYRN DSLYREEELT QLKDTTYTYK WEKVESGSYS FEVVDENNIT YAVTYNHTTP
FAHTFDTYLD KDAKPKPITG FQSNIDILIK YNSRENTFSL VKTRFKRLIV DITDYGYEKI
NRLQITGTFN NWEIEEVPLK SAGENKYEIV LAVKEGNYEY KLIFDEKWVP EKDNLILIVG
ESGALFPKGE LGTGKLSYDA LDKNQTEKAI KHDFRKLNYL NKISENEVEF TIRTQLHDVE
RAYISVDLNE KDIYEKIYEL ERHSDFTHSF DYFKRSISFE EDVKEFSYVF ILEDGNTKYY
FDGKLSNKKG RKIKINFEKD KIEIFYIPNW AKEAIWYNIF PDRFYNHSCY NNPIFNEFGP
ENFEINKLHE SNFEEMYKWN TEEETLGKFD TNRWTSDFSE KTDWEIKGES GKNTSLKYAR
MYGGDLQGIR EKIPYMKELG INAVWLNPVF YSYQNHKYGT NDFRHISPDL GTIRTSGSRY
NAEIDENNPY GDKSYVDILK KNAKDNSELK LLELKLTGEN KGKNGYGETE DPSTWIWTES
DLIMVDLIKE LHRNGIRVIF DGVFNHSSNR HWSFNQVLME GENSKYKNWY KFSDFSKHIK
IEDGMSEEEA YKILNKNREN IKYSGWAGFD SLPEFNSYNL EFKSYIFNIT KKWLLGPDAK
VSKNWYEDDG IDGFRLDVPN CLENQDFWIE WREVVKSTKK DTYITAELWG NASYDINQGN
KFDAVMNYEW LKTVIGYFIN QGYEKNKSYK LKAGEFLNEL REKRTWYPKQ AIQASQNLNG
SHDTDRLLSR IVNDRVGRDL EEGKQLEQGY NGIRPDLASN YHPNTTIDWR SSFIKPKDVL
KLISVFQMTY VGAPMLFYGD EIGMWGATDP YCRKPMLWDE FTYDNEKNPS LTNENEVYSQ
EPDQDLLFWY KKVIKIRKEN PVLVYGKFKE LYWDDGRDIV AYVRSNPNSV IITVLNNSFN
DYEDLEIVTD EPEERYIDLL TGKNIYSRKD GKIILSIRAK QGMILKKWKK SI
//
