ID R5SFR2_9CLOT Unreviewed; 696 AA.
AC R5SFR2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Alpha amylase catalytic domain protein {ECO:0000313|EMBL:CCZ52565.1};
GN ORFNames=BN771_01257 {ECO:0000313|EMBL:CCZ52565.1};
OS Clostridium sp. CAG:75.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262836 {ECO:0000313|EMBL:CCZ52565.1, ECO:0000313|Proteomes:UP000018032};
RN [1] {ECO:0000313|EMBL:CCZ52565.1, ECO:0000313|Proteomes:UP000018032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:75 {ECO:0000313|Proteomes:UP000018032};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCZ52565.1}.
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DR EMBL; CBAE010000202; CCZ52565.1; -; Genomic_DNA.
DR AlphaFoldDB; R5SFR2; -.
DR Proteomes; UP000018032; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11353; AmyAc_euk_bac_CMD_like; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF210; MALTODEXTRIN GLUCOSIDASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF03358; FMN_red; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000018032}.
FT DOMAIN 26..340
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 454..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 77700 MW; 89F5E203BF798B63 CRC64;
MMKWYDQAVF YHIYPLGLCG CAKENTGIAE SHFDQLKEWA EHAAKLNCTA IYIGPLFESV
GHGYETTDYR RVDCRLGTND DFRDYVAYCH KLGLRVIVDG VFNHVGREFF AFKDVQQNRE
QSPYCSWFCN LNFGGNNEYN DGFSYENWGG YNLLVKLNQQ NPEVQNYIFD AIRFWVAEFD
IDGIRLDAAD VLDHGFMHAM RQMTDAMKPD FWLMGEVIHG DYSRWVNDGM LHSVTNYELH
KGLYSGHNDH NYFEIAHSVK RLLGICGDYR LYTFMDNHDV ERIYSKLNNK EHMGLVTLLV
YTLYGIPSMY YGSEFGIEGK KEQGSDWNLR PHLGLADYAD AYTNNPITAL CVKLGELKKQ
YPELSEGQYQ ELSLTNRQFA YARALSETAM ITLLNCDDVS TTITVQAPVG ASSATDMLGQ
AEHVQYENGQ LQVTLPANCG TVIYLGEKVE PITTEKVSSD TEEPIAAEKV STETEEPIAA
GKVSSEKNAE PSYVLLLNGS PHCNGSTATA LEEVAGALER NGVHTEIVQV GHLAVRSCMA
CGACAETGKC VIDDIVNEIA PKFEKADGLV VGSPVYYASA NATLVACLTR LFYSTHFDKR
MKVGASVVSA RRGGCSASFD ELNKFFTISG MPVASSQYWN SIHGNNADEA KQDGEGLQIM
RTLGNNMAFL IKSIAMGKEM FGLPELEERI GTNFIR
//
