ID   F3Z268_DESAF            Unreviewed;      1102 AA.
AC   F3Z268;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   ORFNames=Desaf_2975 {ECO:0000313|EMBL:EGJ51277.1};
OS   Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfocurvibacter.
OX   NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ51277.1, ECO:0000313|Proteomes:UP000007844};
RN   [1] {ECO:0000313|EMBL:EGJ51277.1, ECO:0000313|Proteomes:UP000007844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ51277.1,
RC   ECO:0000313|Proteomes:UP000007844};
RX   PubMed=21642452; DOI=10.1128/JB.05223-11;
RA   Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA   Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA   Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA   Elias D.A.;
RT   "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT   africanus Strain Walvis Bay.";
RL   J. Bacteriol. 193:4037-4038(2011).
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; CP003221; EGJ51277.1; -; Genomic_DNA.
DR   RefSeq; WP_014260933.1; NC_016629.1.
DR   AlphaFoldDB; F3Z268; -.
DR   STRING; 690850.Desaf_2975; -.
DR   KEGG; daf:Desaf_2975; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_0_7; -.
DR   Proteomes; UP000007844; 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:UP000007844}.
FT   DOMAIN          19..418
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1102 AA;  126879 MW;  07F180E48C247649 CRC64;
     MPKKEVQSAH WYKDAVIYQL HIKSFCDGNS DGIGDFKGLI SQLNYLENLG VTAIWLLPFY
     PSPLKDDGYD IADYTAVNPD YGTLADFKRF LKEAHGRDMR VITELVLNHT SDQHEWFQRA
     RKAKPGSAAR DFYVWNDTPD RYSEARIIFQ DFEHSNWSWD PVARAYYWHR FYAHQPDLNY
     DNPKVHAAML RALDFWFDLG VDGLNLDAVP YLYERESTNC ENLPETYGFL KKLRAHVDAR
     HKDKLLLAQA NQWPEDAVSY FGDGDACHMA FHFPLMPRMF MALEMENRYP VLDILDQTPH
     IPASCQWALF LRNHDDLTLE MVTDEERDYM YRIYATDPRA RINLGIRRRL APLLGNDRRK
     IELMNVLLMT LPGSPVLYYG DEIGMGDNYY LGDRDGVRTP MQWSADKNAG FSTANPQKLF
     LPVVIDPEYH YEALNVETQT VRRSSLLWWM RRLISLRTRF EVFGRGSIEF LLPDNVKVLA
     FVRRLEDEIV LVVANLSHHA QMVELDLPDF KWFQPEDIFS RVRFRDISEE PYVLTLSPFA
     YYLFRLHPPR TTTAERTAAE LPRVRAAGWE SLFESREAVR ELEGSVLPRF IRQQRWYGGK
     ARHVREMRIL ERIPISVRNP AIILLVKVVY TEGDPEIYIL PLSFAALGDA EQELPKGTLA
     WAEFADSRGA IYEALHNSDF LCDLLYLMAG RKRLGAREGR LQASAGRHLL QVLAGEDVSL
     EPRLLGAEQS NTSVLFGGSL ILKLYRRTEQ GIHPDLEIAR FLTDKAKFAH TPPFAGAIEY
     RTRGGETLVL GLMQKFIPNQ GDAWEHALDL AMRYFERVQE LAPEARNSPP APPATLLEAA
     EMRLPAPLDG VMSGASLEMA ELLGKRTGQM HVALASDDHS ESMRPTPFST LYQRALFQSM
     QNLARGELRL LRRTLDQLPE AVRGDAKAVL ALEARIIERM RGITSRRIKA QKIRIHGDYH
     LGQVLYTGKD FVIYDFEGEP SRPLSERRLK RSPMRDVGGM IRSWHYAAYS ALLNHPSIQQ
     DEQSDFAPWA DLWYLFMGGR FLRGYLEAMR SSPLIPSDME QLGNMLVPFM LEKAVYEMGY
     ELNNRPDWLI IPLRGIMYLC GE
//