ID   Q5NXV9_AROAE            Unreviewed;      1114 AA.
AC   Q5NXV9;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
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=ebA7001 {ECO:0000313|EMBL:CAI10105.1};
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI10105.1, ECO:0000313|Proteomes:UP000006552};
RN   [1] {ECO:0000313|EMBL:CAI10105.1, ECO:0000313|Proteomes:UP000006552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1 {ECO:0000313|EMBL:CAI10105.1,
RC   ECO:0000313|Proteomes:UP000006552};
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI10105.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5NXV9; -.
DR   STRING; 76114.ebA7001; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; eba:ebA7001; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_4; -.
DR   Proteomes; UP000006552; 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:UP000006552}.
FT   DOMAIN          27..421
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1114 AA;  126097 MW;  DB06C10C1466BA67 CRC64;
     MDLLPAMAAP DKETDDGLWY KDAVVYELHV KAFFDANDDG VGDFNGLTRK LDYIRDLGVN
     TIWLLPFYPS PLKDDGYDVA DYHGVLPAYG TRADFRQFVR EAHRRGLRVI TELVVNHTSD
     QHAWFQAARR APAGSSKRNY YVWSDDPTRY SGTRIIFTDT ETSNWAWDPV AKSYYWHRFF
     SHQPDLNFEN PNVLKAVLRT MRFWLDMGVD GFRLDAIPYL REREGTNNEN LPETHDVIRE
     IRKCIDAHYR GRVLLAEANQ WPEDVREYFG DGDECHMAYH FPLMPRLFMA VAQEDRFPVV
     DIMRQTPDIP ENCQWAIFLR NHDELTLEMV TDRERDYMWQ FFANDPRMRI NVGIRRRLAP
     LLENSRDRVE LMSFLLLTMP GSPILYYGDE LGMGDNVFLG DRDGVRTPMQ WTPDRNAGFS
     RADPQQLYLP PIMDPIYGFQ AINVEAQARN PHSLLNFTRR LIAMRNSSRA FGRGMLRFLE
     PGNRKVLAYL REYRDQSVLC VANLARTPQA VELDLARFEG RVPVEIVGRV PFPPVGKLPY
     LLTLAGHGFF AFELSADAPP PNWHEERLPQ TELPILVLTE GWRTFFRGHQ GGSAVRRAIA
     TRSRDQLQNE VLLPYLQARR WFAAKGETVT RIEVVEEQEW AAGGGNWLLA LLEVSLASGS
     SHLYFLPLGI AWETAGDNPV DRFGAAALAR VREKARIGIL YDAFIDPVYC RALGQSMGGG
     GPQPLGGGSL RFTASEHYAR FAEALGDEVR QPLQEQTNTG VFFGSRLYLK GYRRLQFGTN
     PEIEVGYFLG SAPEFSRVAA VAGSVEYIAP DGRVAALAML QEFVDNQGNA WDYTLNHLDR
     LFSPDTWPAA AADEPEAEGM DRVYLLLAQT LGRRIGEMHA AFAHGTDPAF VPEPLGDAEV
     EAWRAQVIGD VERTLSLLEA ALPRLDERAR DEARQVLAAH HLLVARLAGL DLASPGLVKT
     RLHGDLHLGQ VLIVQNDFVI VDFEGEPARS IDERRCRHSP LRDVAGMLRS FDYAVRTVGY
     HHLQARPEHA EALARALPEW KEGVVRSFMQ AYGEVVAPLP SVPPDAAVAA DFVTLFVIEK
     LLYELRYELD NRPEWVRIPL SALAEIAASP QGSH
//