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Database: UniProt
Entry: Q1QNB0_NITHX
LinkDB: Q1QNB0_NITHX
Original site: Q1QNB0_NITHX 
ID   Q1QNB0_NITHX            Unreviewed;      1088 AA.
AC   Q1QNB0;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619};
DE            EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
GN   OrderedLocusNames=Nham_1465 {ECO:0000313|EMBL:ABE62287.1};
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE62287.1, ECO:0000313|Proteomes:UP000001953};
RN   [1] {ECO:0000313|EMBL:ABE62287.1, ECO:0000313|Proteomes:UP000001953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14
RC   {ECO:0000313|Proteomes:UP000001953};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001595};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR   EMBL; CP000319; ABE62287.1; -; Genomic_DNA.
DR   RefSeq; WP_011509978.1; NC_007964.1.
DR   AlphaFoldDB; Q1QNB0; -.
DR   STRING; 323097.Nham_1465; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; nha:Nham_1465; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_2_5; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001953; Chromosome.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   InterPro; IPR012811; TreS_maltokin_C_dom.
DR   NCBIfam; TIGR02457; TreS_Cterm; 1.
DR   NCBIfam; TIGR02456; treS_nterm; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABE62287.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001953}.
FT   DOMAIN          27..426
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1088 AA;  124193 MW;  C618A14D2E627AF1 CRC64;
     MNEMTKIDAD RYVQTDDLWY KDAIIYQLHV KAFADSNNDG IGDFAGLTNK LDYLQELGVT
     TLWLLPFYPS PGRDDGYDIA DYGSVNPDFG TMKDFRRFIS EARRRGLRVI TELVINHTSD
     QHRWFKRAQR SPPGSSARNW YVWSDTDKKY QDTRIIFTDT EKSNWAWDAE AKAYYWHRFF
     THQPDLNFDN PRVVRAVIQV MKRWLDAGVD GFRLDAIPYL CERDGTNNEN LPETHAVIKH
     IRAELDAYAK GKVLLAEANQ WPEDVQSYFG DGDECHMAYH FPLMPRIYMA IAQEDRFPIT
     DILRQTPDIP PNCQWAMFLR NHDELTLEMV TDIERDYLWS IYAADPRARI NLGIRRRLAP
     LMDNDRRKIE LMNSLLMSFP GTPIIYYGDE IGMGDNIYLG DRNGVRTPMQ WTPDRNGGFS
     RCDPARLYAP PVMDAVYGYE SVNVEAQSRS LFSLLNWMKK LISVRKSSHV FGRGTMSFVR
     SSNRSVLAYV RKNNDEVVLC VANLSRSAQA SELDLSHWKG RSPIEMLGRT TFPDIGELPY
     LITLAPYGFY WFRLTEKPPS PNVAAVIVPD YETLVVPLGA TWMSLARTRS IFERDVLPSH
     LARSRWFPER SASAIAARVP AAIPLMKDQV SRPWLVIFDV THRGQSGRYA MPIRIRWDRL
     DRRNYDAKNI AAVRQGSREG TLIDAAYEND LIAGIIDGLR HRTTFEEGEL RLAYHPTERL
     ASIAEEPIGN VRAVQTEQSN STALVDQRFV VKIYRKLENG INPEVEVGRF LTDVAGFANT
     PALLGSAELT GPDVQAAVAI VHAFVGNQGD AWTVSNAALD RFIDEQRLVG ASDSAPALEE
     KAAYQRSMKQ IGKRVAEMHV ALASRNDIAN FRPEPVTPSD LAHLIDRLMM RAGQTFDRLA
     QVKLADSDRL LADEILSIRP TLHGRLTELL PPSIQMYNIR HHGDFHLGQI LVVRDDVFII
     DFEGEPRRSL PERRLKAPAA RDVAGLIRSI DYSVTTAQER VLKTGTDDDG RLAEALSAWR
     NEATQTFLTA YREAMSDPRL WPQDNDHADR TLRFFLLEKA FYEIDYELAH RPDWLRVALG
     GALRVLRK
//
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