ID   D5BVZ7_NITHN            Unreviewed;      1110 AA.
AC   D5BVZ7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Maltokinase {ECO:0000256|ARBA:ARBA00013882};
DE            EC=2.7.1.175 {ECO:0000256|ARBA:ARBA00011962};
DE            EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
DE   AltName: Full=Maltose-1-phosphate synthase {ECO:0000256|ARBA:ARBA00031251};
GN   OrderedLocusNames=Nhal_2491 {ECO:0000313|EMBL:ADE15576.1};
OS   Nitrosococcus halophilus (strain Nc4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE15576.1, ECO:0000313|Proteomes:UP000001844};
RN   [1] {ECO:0000313|Proteomes:UP000001844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG   US DOE Joint Genome Institute;
RA   Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA   Klotz M.G.;
RT   "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT   aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+);
CC         Xref=Rhea:RHEA:31915, ChEBI:CHEBI:15378, ChEBI:CHEBI:17306,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63576, ChEBI:CHEBI:456216;
CC         EC=2.7.1.175; Evidence={ECO:0000256|ARBA:ARBA00001537};
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 aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR   EMBL; CP001798; ADE15576.1; -; Genomic_DNA.
DR   RefSeq; WP_013033436.1; NC_013960.1.
DR   AlphaFoldDB; D5BVZ7; -.
DR   STRING; 472759.Nhal_2491; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; nhl:Nhal_2491; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001844; 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; IPR040999; Mak_N_cap.
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; PF18085; Mak_N_cap; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT   DOMAIN          24..423
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1110 AA;  128361 MW;  FFCD3E719AE5B8DC CRC64;
     MNQQGEEFSW QDDPLWYKEA IIYQLHVRAF LDSNNDGTGD FQGLTQKLDY IQDLGVNTIW
     LLPFYPSPLR DDGYDIADYR NIYPDYGTRR DFRNFVRAAH RRGLRVITEL VINHTSDQHQ
     WFQAARKAPP GSAKRNFYVW SNSDQKFPET RIIFTDTETS NWAWDPVAKA YYWHRFFSHQ
     PDLNHNNPQV VKAVIRVMRF WLDMGVDGLR LDAIPYLCVR EGTHNENLPE THEVLKQMRA
     VVDDHYRHRM FLAEANQWPE DVREYFGDGD ECHMAYHFPL MPRMYMAIAQ EDRHPITEIM
     NQTPDIPESC QWAIFLRNHD ELTLEMVTDK ERDYMYQTYA TNPRMRVNVG IRRRLAPLMD
     NDLDKIQLMN SLLLSMPGSP IIYYGDEIGM GENIYLGDRN GVRTPMQWSP DRNAGFSKAD
     PQRLYLPPIM DPIYGYEAVN VEAQSRDPSS LLNWMKRLLA VRKNTQAFGR GTLKFLRPGN
     RKILAYVREY GGEAILCVAN LSRYAQPVEL DLSRFKGRVP LEMMGHTPFP PIGELPYLLT
     LPSHGFYWFR LATDVEEPSW HEERLPPLEL PVLVLFAGWD SLFPSRVDPP RKRMSEKLCG
     QLEQLLRDFL ITQRWFAAKG EEVERVRLEQ MEEWTEEAGS WLLARVRVEF ADIEVQSYFI
     PLALAWGEGD EEPIRRLLPS TIAKIRRQAR IGILYDALAD VSFSRALVTA MGQHREIPFG
     AGKLKFSPTA AFEKLVNGVS LQQLWRPAME GTNSTLILDN RLFLKIYRHL QEGINPEQEM
     GHFLTEASPF PNIVPLAGTL ESLGPEGTPM TLALLQGFVP NQGDAWAYTV DYLERFLENS
     LAKPLEEAAI EFGETHNNYL RMIRILGQRT GELHQALAKE TGNPAFDPEP INSADLDSWR
     KHIEKDIEQT LKMLEQRRSE FSEPLRTEVD CLLALKETLR QRLALIPPEL RAVKTRYHGD
     YHLGQVLVAE DDFVIIDFEG EPARPLAERR IKHSPLRDVA GMLRSFNYAT AVALRHCTVE
     RPEDRGLLLP LAHTWERQVG ESFLAGYGEA AAGCPSYPAD PEHAHYLIEL FILEKALYEL
     RYELDNRPEW VDVPLNGLLE FLEEEENPGE
//