ID A0A1G9NW81_9BACT Unreviewed; 1108 AA.
AC A0A1G9NW81;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN05421823_1093 {ECO:0000313|EMBL:SDL90862.1};
OS Catalinimonas alkaloidigena.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Catalimonadaceae;
OC Catalinimonas.
OX NCBI_TaxID=1075417 {ECO:0000313|EMBL:SDL90862.1, ECO:0000313|Proteomes:UP000198510};
RN [1] {ECO:0000313|EMBL:SDL90862.1, ECO:0000313|Proteomes:UP000198510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25186 {ECO:0000313|EMBL:SDL90862.1,
RC ECO:0000313|Proteomes:UP000198510};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNFO01000009; SDL90862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9NW81; -.
DR STRING; 1075417.SAMN05421823_1093; -.
DR OrthoDB; 9806009at2; -.
DR Proteomes; UP000198510; Unassembled WGS sequence.
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:0016740; F:transferase activity; 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:UP000198510};
KW Transferase {ECO:0000313|EMBL:SDL90862.1}.
FT DOMAIN 23..422
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1108 AA; 129219 MW; 0A72CCD94A658981 CRC64;
MSKARKEKKD ANLLWYKDAI IYELHIKAFK DSNGDGIGDF KGLMQKLDYL QNLGVTAIWL
LPFYPSPLRD DGYDIADYYS INPSYGTIRD FKNFLKEAHA RGLKVITELV INHTSDRHPW
FQRAREAKPG SPYRDYYVWS DDPHKYKDTR IIFQDFEASN WTWDPVAKAY YWHRFYSHQP
DLNFDSPRVQ QEVFKMIDYW ADMGVDGFRL DAIPYLFERE NTNCENLPET HDFLKKLRAH
LDSKYDDKMF LAEANMWPEQ AASYFGDGDE CHMNFHFPIM PRLFMAVKME DRHPIIDIME
QTPDIPSNCQ WAMFLRNHDE LTLEMVTDEE RDYMYKVYVR DPMARINLGI RHRLAPLLEN
DRRKIELMNV LLFSLPGTPV LYYGDEIGMG DNYYLGDRDG VRTPMQWNAD RNAGFSDANP
QQLYLPVILD PEYQYESVNV ENQQRNQNSL FWWMKRSIEM RKRHVAFGRG DIRFLQTSNA
KVLAFVRCYE DEAILVVVNL SRFAEAVDLD IPEFKGYVPH EIFSKNKFPY ITRDQYPLTL
APFGYFWFQL KTERAGLEAE SLGAEPMLEL DRWETIFDEG SRRVLVEEIL PTYLFRCRWF
GGKARVVQKM DILELLPMGD KGEQMALAIL EVTYNEGLPE LYQLPLSVAA NESRVEQLQE
QSPQALIAPI AVRGFNTMLY DGVYDEAFRQ YLFKGLTKRR RVKLDGSELV FSAAKQVGRN
EAVGMARSRV LSAEQSNTSI IYQDKYFLKI YRKLDHTINP DLEITRFLTE KAGFPNTPKF
LGSAELQRGK AAIVLAMMQE LASNQGDAWT YFNDSLRRYF ERVIAVSEKT KVPPLIGSLT
EPASFEEMPE VLKNIIGGAY VERVGLLAQR TAEMHIALAS RPKDEGFEPD AFSLHYQRSL
YSSLQGLVKN NYASLKKQLS KLPEAWVDDA KAVLATREEA LATMKRIYSH KFEAMKIRNH
GDYHLGQVLF TGKDFVIIDF EGEPARSFSE RRLKRSPLRD VAGMIRSFHY AAYNALFQQE
SANQSEFEPW AEQWYHYISG FFMRRYLKAV QGYDFIPEDK DDLNLLLQIF LLEKAVYELG
YELNNRPNWV GIPLRGIRKL LEDSKNEE
//
