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Database: UniProt/TrEMBL
Entry: Q2RTZ0_RHORT
LinkDB: Q2RTZ0_RHORT
Original site: Q2RTZ0_RHORT 
ID   Q2RTZ0_RHORT            Unreviewed;      1100 AA.
AC   Q2RTZ0;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   13-SEP-2023, entry version 110.
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=Rru_A1605 {ECO:0000313|EMBL:ABC22405.1};
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22405.1, ECO:0000313|Proteomes:UP000001929};
RN   [1] {ECO:0000313|EMBL:ABC22405.1, ECO:0000313|Proteomes:UP000001929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC   {ECO:0000313|Proteomes:UP000001929};
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC22405.1; -; Genomic_DNA.
DR   RefSeq; WP_011389295.1; NC_007643.1.
DR   RefSeq; YP_426692.1; NC_007643.1.
DR   AlphaFoldDB; Q2RTZ0; -.
DR   STRING; 269796.Rru_A1605; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABC22405; ABC22405; Rru_A1605.
DR   KEGG; rru:Rru_A1605; -.
DR   PATRIC; fig|269796.9.peg.1681; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_5; -.
DR   OMA; QEDRFPI; -.
DR   PhylomeDB; Q2RTZ0; -.
DR   Proteomes; UP000001929; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABC22405.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001929}.
FT   DOMAIN          14..409
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1100 AA;  123820 MW;  67B06B768CB9B9C8 CRC64;
     MSDFLWYKDA IVYQLHVKAF FDSNGDGFGD FKGLTEKLDY LSDLGVTAVW ILPFYPSPLR
     DDGYDIADYK AIHRAYGTMG DFRRFVREAH ERGLKVITEL VINHTSDQHA WFQRAREAKP
     GSKARDMYVW SDTDQRYLDT RIIFTDTETS NWAWDPLAKA YYWHRFFAHQ PDLNWDNPRI
     FEEITRVMKF WLDCGVDGMR LDAIPYLVER DGTNNENLPE THVVLKRLRA WLDAHYEDRM
     FLAEANQWPE DVREYFGEAG DECHMAFHFP VMPRIYMAVA QEDRHPITDI MRQTPEIPAA
     CQWAIFLRNH DELTLEMVTD RERDYMNTFY ANDSRARINV GIRRRLAPLL DNDRRKIELL
     NSLLMSMPGT PIIYYGDEIG MGDNIFLGDR DGVRTPMQWS PDRNGGFSRA DPASLYLPTI
     MDAVYGFFAV NVEAQSRSPS SLLNWMRRLI AVRKRHPSFG RGTLRFLYPG NRKILAYLRE
     FEGEVILCVA NLSRAPQPAE LGLAEFSGRV PVEMLGNSVF PPIGELHYFI TLPAYGFYWF
     RLSKGEGPSW HEPPVEPLPD LSTLVLPRIW DSLGSDGPLR QIQGDILPAF LPKQRWFSGK
     EHSLRGVEMT DHAVISAPGA ASGWMLALWR ADYKDGAPGQ TFQLPLDIAW ESREDDPLSR
     LLPFTLARVR RVNRVGALYD AMAGPAFPLA LVQAMAEGAN VTTAKGGGLR FTRTQAFPAG
     PLPGPEAVAR LGREQSNTSI KLGEDMVLKL YRRVEAGIHP EIEIGRFLTD VAGFANAPPL
     LGALEHIDAK GAISALAVLQ GFVRNQGDGW DYMLAYLDRF LDDRAQAPAE VGEGGGPAGS
     PHGIIHAQAD ILGQRVAELH HAFATPTEDP AFSAEAVGPE DLASWREQVR TQAAQARQAL
     DTALPGLSAE VAGLVTRLLD CWERIDARVD APISLAEGLV KTRIHGDLHL GQVVVVRDDF
     HILDFEGEPV KGLSERRDKH CPLKDVAGML RSFDYAAWSA ALSFRQTHAE VRIDVLPALG
     VWQEEIREAF LAGYDRAIAG CPSVPALEEG RRDLLSLFML EKALYEVSYE AANRPDWLRI
     PIGGVLRLLG EGPSDEIKPR
//
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