ID A5G2P3_ACICJ Unreviewed; 1110 AA.
AC A5G2P3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=Acry_2935 {ECO:0000313|EMBL:ABQ32125.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ32125.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ32125.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ32125.1,
RC ECO:0000313|Proteomes:UP000000245};
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., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ32125.1; -; Genomic_DNA.
DR RefSeq; WP_012040421.1; NC_009484.1.
DR AlphaFoldDB; A5G2P3; -.
DR STRING; 349163.Acry_2935; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; acr:Acry_2935; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_1_5; -.
DR Proteomes; UP000000245; 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:ABQ32125.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245}.
FT DOMAIN 28..427
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1110 AA; 125410 MW; 4D79586CF50304FD CRC64;
MTSLTDQIIR PQANMFDPLW YKDAVIYQVH VKSFFDKNND GVGDFAGLTE KLDYIAELGV
TAVWILPFYP SPRRDDGYDI SAYRAVHPEY GSLGDLRRFI DAAHRRGLRV ITELVVNHTS
DQHPWFQRAR HARPGSSARN YYVWSDTDRK YDGTRIIFLD TEKSNWTWDP VAGAYYWHRF
YSHQPDLNFD NPRVLQEVLG IMRFWLDLGV DGMRLDAVPY LIERDGTNNE NLPETHAILK
QIRAALDAHA PGRMLLAEAN QWPEDARPYF GEGDECHMAF HFPLMPRMYM AIAQEDRFPI
SDIMRQTPEI PENCQWAVFL RNHDELTLEM VTDKERDYLW ETYAADRRAR INLGIRRRLA
PLLERDRRRI ELMNGLLLSM PGTPVIYYGD EIGMGDNIHL GDRDGVRTPM QWSPDRNGGF
SRADPAALVL PPIMDPLYGY QALNVEAQAK DPYSLLNWMR RMLAVRRRHR AFGRGGLRFL
YPGNRKVLAY VREWTDQDGG EETILCVYNL ARTAQAVELD LAAFGGRIPL DLIGGAPFPP
VGQLPYMLTL PPFAFYWFSL TTEAAMPFWR IQPSEPLPDY ITLVMRLGLA DLVAVDSRHS
LETEILPPYL QRRRWFAAKD RHVRSVTIAN AHMLGTAEDD FLLCEIEVEF AGEGRGDVYL
LPLAVVWDDG PVASIVQQLA LARIRRHRRV GYLTDAFAVD RFCHDIIARL RTKSCISLAS
GRLSYEPTAL IDDLPPLDDA EIRRFSAEQS NSSLIVGDAA VMKILRRTER GIHPETEMSR
FLTDASFANI PALLGEVVRL DPDGERRTLI VVQQFVRNQG DAWQWTLDVL GRAVDGAIHA
ELRDPGGIDP LSGYLSFVSV IGRRLAEMHS VLAQFGTGPD FAPERAGEAE IAAWAEGAKG
QLDAAVAAVE QMADRAGPET QGLIRRLRDE RTAIETRLRR LAEAGAGTLL TRVHGDFHLG
QVLVAQGDAF IIDFEGEPIK PIAERRKKSS PLRDVAGLLR SLDYAAATVE RAAFAASERG
EDRQQAMIAR FRTDAAAAFI EAYRAVAMTA PRPWITEVAW RDVLALFMIE KAAYEICYEA
ANRPGWIDIP LSGLVRIHER HEGGGDAGIG
//
