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Database: UniProt
Entry: Q82T86_NITEU
LinkDB: Q82T86_NITEU
Original site: Q82T86_NITEU 
ID   Q82T86_NITEU            Unreviewed;       670 AA.
AC   Q82T86;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Glycosyl hydrolase family 57 {ECO:0000313|EMBL:CAD85943.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAD85943.1};
GN   Name=amyA {ECO:0000313|EMBL:CAD85943.1};
GN   OrderedLocusNames=NE2032 {ECO:0000313|EMBL:CAD85943.1};
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD85943.1, ECO:0000313|Proteomes:UP000001416};
RN   [1] {ECO:0000313|EMBL:CAD85943.1, ECO:0000313|Proteomes:UP000001416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC   {ECO:0000313|Proteomes:UP000001416};
RX   PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA   Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA   Whittaker M., Arp D.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC       {ECO:0000256|ARBA:ARBA00006821}.
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DR   EMBL; AL954747; CAD85943.1; -; Genomic_DNA.
DR   RefSeq; WP_011112548.1; NC_004757.1.
DR   AlphaFoldDB; Q82T86; -.
DR   STRING; 228410.NE2032; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   KEGG; neu:NE2032; -.
DR   eggNOG; COG1449; Bacteria.
DR   HOGENOM; CLU_026700_0_0_4; -.
DR   OrthoDB; 8476at2; -.
DR   PhylomeDB; Q82T86; -.
DR   Proteomes; UP000001416; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10793; GH57N_TLGT_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.110.20; -; 1.
DR   InterPro; IPR015179; A-amylase/a-glucTrfase_C.
DR   InterPro; IPR015178; A-amylase/a-glucTrfase_central.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR004300; Glyco_hydro_57_N.
DR   PANTHER; PTHR36306:SF1; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR   PANTHER; PTHR36306; ALPHA-AMYLASE-RELATED-RELATED; 1.
DR   Pfam; PF09094; AmyA-A_glucT_m; 1.
DR   Pfam; PF09095; AmyA-gluTrfs_C; 1.
DR   Pfam; PF03065; Glyco_hydro_57; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000313|EMBL:CAD85943.1};
KW   Hydrolase {ECO:0000313|EMBL:CAD85943.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001416}.
FT   DOMAIN          26..273
FT                   /note="Glycoside hydrolase family 57 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03065"
FT   DOMAIN          316..394
FT                   /note="Alpha-amylase/4-alpha-glucanotransferase central"
FT                   /evidence="ECO:0000259|Pfam:PF09094"
FT   DOMAIN          408..663
FT                   /note="Alpha-amylase/4-alpha-glucanotransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09095"
SQ   SEQUENCE   670 AA;  76614 MW;  7CA73A9594F07C7B CRC64;
     MTSSVSFLFG VHAHQPIGNF PEVVIDAHER CYKPFLHTLH RYPEFRFAVH FSGWLLDFLF
     EHYPQDMALL REMVTRGQVE LFGAGDTEPV LAAIPERDRV GQLRTFSTKL KKKLGQRPQG
     AWLTERVWES TVIPALTRCG IRYVIVDDYH FICAGKRKTE LDGFFTTEED RHSLDLFPIS
     EALRYRLPFS PAQEAIAYIE SLTDQATTGR QPAAVYFDDI EKFGIWPETY QWVYERGWLE
     QFIQGVLASP RIRMQHYRDY HASEKTRGIL YLPTTSYIEM NEWTLPAEPA HTYADLVQQA
     KAAGWYEPNK SFLRGGIWKN FFSRYPESNW MHKRMLGLSA RYARLPASQR TDAMQQCLYA
     SQANDAYWHG LFGGLYLPHL RRAVYNNLIE LEALLDQCVP RTARYQEDID LDGTEEIHLQ
     NGIVQIILKL DGGASICELD TYPLKHNFAD TLTRQTEHYY RKIRLNSGEN STHDQSGIAS
     AHDRVSFKHK IGHADLEPDP HAQSLFIDRL NGESLHYQLQ PSTREDEIIF QTVAGAGLIH
     KYFRISANRL LVTYECTNEV AGHMQTEINL AMPSCDGPGG RYVRDRIALS GFGSAIELGD
     LTALTLEDDT LGGNLSLKIS SAATFHACPH FTVSQSEGGF EKIMQAAKLT LTWPVTTREQ
     RITLQFDKKR
//
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