ID A0A0D5LZT5_9GAMM Unreviewed; 1115 AA.
AC A0A0D5LZT5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=KO116_01191 {ECO:0000313|EMBL:AJY49684.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY49684.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY49684.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY49684.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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; CP011052; AJY49684.1; -; Genomic_DNA.
DR RefSeq; WP_045812081.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5LZT5; -.
DR STRING; 1504981.KO116_01191; -.
DR KEGG; hak:KO116_01191; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_2_0_6; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000028645; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AJY49684.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 30..429
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT COILED 899..933
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1115 AA; 126953 MW; AC1CBD1AE219CE68 CRC64;
MMDASSETHA VEAMDFLDDP LWYKDAVIYQ VHVKAFFDAN DDGIGDFEGL IQKLDYIVSL
GVNTIWILPF YPSPRRDDGY DIAEYTSVSP DYGTLDDAKR FIQEAHQRGL RVITELVINH
TSDQHEWFQR ARQAPAGSPE RDFYVWSDTD QKYPGTRIIF LDTESSNWTW DPVAGAYFWH
RFYSHQPDLN FDNPVVLDEI LKVMEYWLDM GVDGLRLDAI PYLVEREGTN NENLPETHVV
LKKIRAVLDE RYPDRMLLAE ANQWPEDTRP YFGDGDECHM AFHFPLMPRM YMALAQEDRF
PITDILRQTP EIPATCQWAI FLRNHDELTL EMVTDKERDY LWNHYAADRR ARINLGIRRR
LAPLLERDRR RIELLNSLLL SMPGTPVLYY GDEIGMGDNI YLGDRDGVRT PMQWSVDRNG
GFSRADPAKL VLPPIMDPLY GYQTVNVEAQ IRDSHSLLSN MRRLLAVRSQ HRAFSRGTMR
PLYPSNRHIL AYLREMTLDN GETETLLCVA NVASTAQAVE LDLSAFSGQV PVEMVGGSAF
PPVGKLAYLL TLPPYGFFWF LLAPATAMPE WHVPVPEPMP DFVTLIIKKR LNEIFEETPR
RLLERETLPS YLPKRRWFAA KQARIEEVHL HATASLEHSG HTLLFSEVEV KHGQGSERYQ
LPLAFLGEDE QSNPLPQQLA MARVRRFHEV GLLTDAVTLD AFTLAVLENM RLGTVLPYEK
GEIHFLPTAT FAELTLPEHL EVVQQSAEQS NSSVIINHQL VLKLFRRLEP GIHPEAEIGS
YLTERGFTHT VPLYGVVTRL EEGATQTLMI LQGFIDNQGD AWSWTRNKLE RAIREAVADD
ERASEPKAEA RYGAFEELAE FATTLGRRLG ELHMVLATPN DDPAFTPEVA GLSHVQHWTQ
RVTQRVEEAL NVLEQHKNTA NEAEQRLADI ILARRATLMD AIKKMSELAQ GSLLTRIHGD
LHLGQVLVAH DDAYIIDFEG EPARPLEERR AKDSPLRDVA GMLRSFDYAY AKVEEARPGD
NEGADTHTGT SHAVVEQYLL KGRQAFLNAY WLATMEIPHE WKQASGAAAA VDLFVLEKTA
YEIAYEAANR PEWLGVPLHG LAALIEQLSP GEPHE
//
