ID   U9VK40_9CYAN            Unreviewed;       603 AA.
AC   U9VK40;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Sucrose phosphorylase {ECO:0000313|EMBL:ESA33034.1};
GN   ORFNames=N836_23510 {ECO:0000313|EMBL:ESA33034.1};
OS   Leptolyngbya sp. Heron Island J.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA33034.1, ECO:0000313|Proteomes:UP000017515};
RN   [1] {ECO:0000313|EMBL:ESA33034.1, ECO:0000313|Proteomes:UP000017515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Heron Island J {ECO:0000313|EMBL:ESA33034.1,
RC   ECO:0000313|Proteomes:UP000017515};
RX   PubMed=24503993;
RA   Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA   Fromme P.;
RT   "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT   Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL   Genome Announc. 2:e01166-e01113(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESA33034.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWNH01000106; ESA33034.1; -; Genomic_DNA.
DR   RefSeq; WP_023076131.1; NZ_AWNH01000106.1.
DR   AlphaFoldDB; U9VK40; -.
DR   STRING; 1385935.N836_23510; -.
DR   PATRIC; fig|1385935.3.peg.6370; -.
DR   eggNOG; COG0366; Bacteria.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000017515; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11356; AmyAc_Sucrose_phosphorylase-like_1; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR033746; GGa_phosphorylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR016377; Sucrose_GGa_phosphorylase-rel.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF214; GLUCOSYLGLYCERATE PHOSPHORYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   PIRSF; PIRSF003059; Sucrose_phosphorylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017515};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          61..466
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         239..241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         348..349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         455
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
SQ   SEQUENCE   603 AA;  68733 MW;  A0B6B8844377CBF7 CRC64;
     MLTTSKATIS FERFTAKVYP LLKSVYSEEQ LDNLLPQLYD LTKEHLKPHS QEDLGKWDQD
     KILLITYGDS ICSDDASPLQ TLHQFLNTRL ADVVTGVHIL PFFPYSSDDG FAVIDFLKVN
     PKLGNWADVE AIGRNFNLMF DLVANHVSSQ SAWFEEFRQN QLPGRDYFIT LPEDTPTADV
     VRPRSSSLLT PVDTAKGLKH VWTTFSADQV DVDYSNPDVF LEFVKIILAY VRHGARYIRL
     DAVGFLWKSL NTSCIHLPET HKLIQTFREI LQMVDPGIAL ITETNVPNRE NLSYFGDRNE
     AHMIYNFSLP PLLLNALMQG RADHLKTWMM SMPPAPIGCA YFNFTASHDG IGLRPTEGLL
     GDHEFKTLID TMRSFGAQIS MRSKADGSES PYEINISLFD ALQGTAQGPD QWQIERFICS
     QTVMMSLEGI PAFYIHSLLA TPNDVEGMKA TGHNRSINRH AWDKQRLDAL LEDPESSQSI
     VLAELSRLIK IRRQQKAFHP NATQYTLHPE NPAIFAFWRQ SIARDQSIFS IHNLSDQCHT
     LRLSELNLVN TDSWMDLISG ESFDNLHAVY ELKPYQSVWL TNRPYYDSSN IPERVDLEFL
     YQA
//