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Database: UniProt
Entry: A1BJE7_CHLPD
LinkDB: A1BJE7_CHLPD
Original site: A1BJE7_CHLPD 
ID   A1BJE7_CHLPD            Unreviewed;      1098 AA.
AC   A1BJE7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=Cpha266_2536 {ECO:0000313|EMBL:ABL66524.1};
OS   Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL66524.1, ECO:0000313|Proteomes:UP000008701};
RN   [1] {ECO:0000313|EMBL:ABL66524.1, ECO:0000313|Proteomes:UP000008701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 266 {ECO:0000313|EMBL:ABL66524.1,
RC   ECO:0000313|Proteomes:UP000008701};
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., Pitluck S., Goltsman E.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL   Submitted (DEC-2006) 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; CP000492; ABL66524.1; -; Genomic_DNA.
DR   RefSeq; WP_011746301.1; NC_008639.1.
DR   AlphaFoldDB; A1BJE7; -.
DR   STRING; 290317.Cpha266_2536; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; cph:Cpha266_2536; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_10; -.
DR   OrthoDB; 9806009at2; -.
DR   Proteomes; UP000008701; 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, ECO:0000313|EMBL:ABL66524.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008701}.
FT   DOMAIN          16..410
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1098 AA;  127120 MW;  74A51524647689BB CRC64;
     MYQPEALWYK DAIIYEAHVK TFYDSNNDGI GDFQGLRQKL GYLESLGITA IWLLPFYPSP
     LRDDGYDIAD YMKVNPDYGT LDDFREFLEE AHSRGLKVIT ELVVNHTSDQ HAWFQRARRA
     PVGSPERNFY VWSDDPNKYS ETRIIFQDFE ASNWTYDPVA GQYFWHRFYH HQPDLNFENP
     EVHQALFDVL DFWLGMGVDG LRLDAVPYLY EAEGTNCENL PQTYEYLKSL RSYVDEHYPN
     RMLLAEANQW PEDAAAYFGN GDQCHMNFHF PLMPRMYMAL ATEDRFPLLD ILDQTPDIPE
     NCQWASFLRN HDELTLEMVT DEERDYMRRV YANDSKARIN LGIRRRLAPL MTNDRRKIEL
     MNIMLLSLPG TPVLYYGDEI GMGDNYYLGD RDGVRTPMQW NADRNAGFSR ANPQKLLLPV
     IIDPEYHYEA INVEVQEGNT NSLLWWMRHT IATARKYKAL SRGTIEFLQV SNPKVLIFTR
     TFEDETVLTV INLSRNAQAV MIDLAAYADC IPEEVFSLNR FPKIRKTPYM VALGAYGYFW
     LKLVKESDES EGRPFLEEPY ASVTRWTNLF ASKNREKLEI DILPKYFMSS RWFGGKARTI
     IRVVIADTIP VEGMENAKML LAEVRYSSGE NELYQLPVCF VPDAMISRHD DNFYKRAIAR
     AVLGDEKGFL CDATYETAFL NQLFRLVMGQ HPWHGKSGQI SGCKGEKADV LCSEECHSSP
     EPALLGNEQS NTSIRYRDRL CLKLYRRIEI GVSPEIDMCR ALTEKTGFSN LPEYLGSLDY
     AQNRASHYSL GILQSYVQNE GNAWNISLDY AQRYYEDVLS KIQSVSELPA LPALGGNPVP
     LPSIMLELIG GPYLGLVEKL GERTAEMHIA LASINDDPQF APEPFTSLYQ RSIYQAMCEQ
     VKRSMMLLRL IKGNIPEEQQ ELVSRLLMSE EDILLQFDPI RREKIDAVKI RIHGDYHLGQ
     VLYTGRDVVV IDFEGEPARP VSERKIKRSA FRDVAGMMRS FDYAAFNALL LNPVIRPEDR
     HRLEPWADLW SFYVSQHFID AYFNAVKGHD IIPEEPDQRE HLLRGYLMNK AIYELNYELN
     NRPEWAMIPL RGILRMLE
//
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