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Database: UniProt
Entry: A0A076MRJ9_AMYME
LinkDB: A0A076MRJ9_AMYME
Original site: A0A076MRJ9_AMYME 
ID   A0A076MRJ9_AMYME        Unreviewed;       493 AA.
AC   A0A076MRJ9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Glycoside hydrolase, family 57 {ECO:0000313|EMBL:AIJ21546.1};
GN   ORFNames=AMETH_1454 {ECO:0000313|EMBL:AIJ21546.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ21546.1, ECO:0000313|Proteomes:UP000062973};
RN   [1] {ECO:0000313|EMBL:AIJ21546.1, ECO:0000313|Proteomes:UP000062973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ21546.1,
RC   ECO:0000313|Proteomes:UP000062973};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC       {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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DR   EMBL; CP009110; AIJ21546.1; -; Genomic_DNA.
DR   RefSeq; WP_017987406.1; NZ_CP009110.1.
DR   AlphaFoldDB; A0A076MRJ9; -.
DR   STRING; 1068978.AMETH_1454; -.
DR   KEGG; amq:AMETH_1454; -.
DR   PATRIC; fig|1068978.7.peg.1532; -.
DR   eggNOG; COG1543; Bacteria.
DR   HOGENOM; CLU_008192_1_0_11; -.
DR   OrthoDB; 9803279at2; -.
DR   Proteomes; UP000062973; Chromosome.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   InterPro; IPR037090; 57_glycoside_trans_central.
DR   InterPro; IPR015293; BE_C.
DR   InterPro; IPR040042; Branching_enz_MT3115-like.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR004300; Glyco_hydro_57_N.
DR   PANTHER; PTHR41695; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR   PANTHER; PTHR41695:SF1; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR   Pfam; PF09210; BE_C; 1.
DR   Pfam; PF03065; Glyco_hydro_57; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361196};
KW   Hydrolase {ECO:0000313|EMBL:AIJ21546.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062973}.
FT   DOMAIN          9..358
FT                   /note="Glycoside hydrolase family 57 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03065"
FT   DOMAIN          412..491
FT                   /note="1,4-alpha-glucan branching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09210"
FT   ACT_SITE        188
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   ACT_SITE        327
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         434
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ   SEQUENCE   493 AA;  54757 MW;  1C343EC2B0D0EFDA CRC64;
     MTGEGTFCLV LHSHLPWLPH HGSWPVGEEW LYQAWAHSYL PVVDLLRRFA AEGRRDVLTL
     GVTPVLAAQL DDPYALRAFH EWLGHWQLRT VQAGTLWRED PLLRELAAAE YRTATRSLED
     FETRWRHGFS PLLRSLVDSG VVELLGGPYA HPFQPLLQPR VRSFMLRGGL ADTELRIGHR
     PAGIWAPECG YAPGMEEDYA AAGVRRFLVD GPSLHGDTAF ARPVGSTDVL CFGRDLAVTY
     RVWSPRAGYP GHANYRDFHT WAHEVGLKPS RVTGKQVEPA DKAPYDPALA ADTLRAHVKD
     FVETVVSRLR ALRSLHGREA LVVAAYDTEL FGHWWHEGPA WLEGVLRALP EAGVRVTTLQ
     GAVSAGLVGA PVELPASSWG SGKDWRVWDG EQVADMVADN AALQQRLLAL PRAETRDRVA
     DWAVGEATMA LSSDWAFMVT KDSAADYARR RAAVHTARFD ELASLIGRGP LPPAVERWAR
     EDNPFGQLDA RQL
//
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