ID M1E1F6_9HYPH Unreviewed; 584 AA. AC M1E1F6; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 27-MAR-2024, entry version 45. DE SubName: Full=Sucrose isomerase {ECO:0000313|PDB:4GIN}; GN Name=mutB {ECO:0000313|PDB:4GIN}; OS Rhizobium sp. MX-45. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1071045 {ECO:0000313|PDB:4GIN}; RN [1] {ECO:0007829|PDB:4H7V, ECO:0007829|PDB:4H8H} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-584 IN COMPLEX WITH CALCIUM, RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-584 IN COMPLEX WITH CALCIUM, RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 28-584 IN COMPLEX WITH CALCIUM RP AND GLUCOSE, AND X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 28-584 IN RP COMPLEX WITH CALCIUM. RA Lipski A., Watzlawick H., Ravaud S., Robert X., Haser R., Mattes R., RA Aghajari N.; RT "Insights into product binding in sucrose isomerases from crystal RT structures of MutB from Rhizobium sp."; RL Submitted (SEP-2012) to the PDB data bank. RN [2] {ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 28-584 IN COMPLEX WITH CALCIUM. RX PubMed=23385465; DOI=10.1107/S0907444912045532; RA Lipski A., Watzlawick H., Ravaud S., Robert X., Rhimi M., Haser R., RA Mattes R., Aghajari N.; RT "Mutations inducing an active-site aperture in Rhizobium sp. sucrose RT isomerase confer hydrolytic activity."; RL Acta Crystallogr. D 69:298-307(2013). 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 PDB; 4GIN; X-ray; 1.90 A; A=1-584. DR PDB; 4H2C; X-ray; 1.70 A; A=28-584. DR PDB; 4H7V; X-ray; 1.80 A; A/B=28-584. DR PDB; 4H8H; X-ray; 2.00 A; A/B=28-584. DR PDB; 4H8U; X-ray; 2.00 A; A/B=28-584. DR PDB; 4H8V; X-ray; 1.95 A; A/B=28-584. DR PDB; 4HA1; X-ray; 2.20 A; A/B=28-584. DR PDBsum; 4GIN; -. DR PDBsum; 4H2C; -. DR PDBsum; 4H7V; -. DR PDBsum; 4H8H; -. DR PDBsum; 4H8U; -. DR PDBsum; 4H8V; -. DR PDBsum; 4HA1; -. DR AlphaFoldDB; M1E1F6; -. DR SMR; M1E1F6; -. DR BRENDA; 5.4.99.11; 5351. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 2. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR022567; DUF3459. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR045857; O16G_dom_2. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF11941; DUF3459; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C}; KW Calcium {ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C}; KW Metal-binding {ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..584 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004014717" FT DOMAIN 41..445 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT BINDING 49 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C" FT BINDING 51 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C" FT BINDING 55 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C" FT BINDING 57 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:4GIN, ECO:0007829|PDB:4H2C" FT CARBOHYD 88 FT /note="Glucose 1" FT /evidence="ECO:0007829|PDB:4H7V" FT CARBOHYD 88 FT /note="Glucose 2" FT /evidence="ECO:0007829|PDB:4HA1" FT CARBOHYD 131 FT /note="Glucose 1" FT /evidence="ECO:0007829|PDB:4H7V" FT CARBOHYD 195 FT /note="Glucose 2" FT /evidence="ECO:0007829|PDB:4HA1" FT CARBOHYD 225 FT /note="Glucose 1" FT /evidence="ECO:0007829|PDB:4H7V" FT CARBOHYD 225 FT /note="Glucose 2" FT /evidence="ECO:0007829|PDB:4HA1" FT CARBOHYD 281 FT /note="Glucose 2" FT /evidence="ECO:0007829|PDB:4HA1" FT CARBOHYD 353 FT /note="Glucose 1" FT /evidence="ECO:0007829|PDB:4H7V" FT CARBOHYD 353 FT /note="Glucose 2" FT /evidence="ECO:0007829|PDB:4HA1" FT CARBOHYD 354 FT /note="Glucose 1" FT /evidence="ECO:0007829|PDB:4H7V" FT CARBOHYD 354 FT /note="Glucose 2" FT /evidence="ECO:0007829|PDB:4HA1" FT CARBOHYD 441 FT /note="Glucose 1" FT /evidence="ECO:0007829|PDB:4H7V" FT CARBOHYD 441 FT /note="Glucose 2" FT /evidence="ECO:0007829|PDB:4HA1" SQ SEQUENCE 584 AA; 66739 MW; E26FB3B877608B86 CRC64; MLMKRLFAAS LMLAFSSVSS VRAEEAVKPG APWWKSAVFY QVYPRSFKDT NGDGIGDFKG LTEKLDYLKG LGIDAIWINP HYASPNTDNG YDISDYREVM KEYGTMEDFD RLMAELKKRG MRLMVDVVIN HSSDQHEWFK SSRASKDNPY RDYYFWRDGK DGHEPNNYPS FFGGSAWEKD PVTGQYYLHY FGRQQPDLNW DTPKLREELY AMLRFWLDKG VSGMRFDTVA TYSKTPGFPD LTPEQMKNFA EAYTQGPNLH RYLQEMHEKV FDHYDAVTAG EIFGAPLNQV PLFIDSRRKE LDMAFTFDLI CYDRALDRWH TIPRTLADFR QTIDKVDAIA GEYGWNTFFL GNHDNPRAVS HFGDDRPQWR EASAKALATV TLTQRGTPFI FQGDELGMTN YPFKTLQDFD DIEVKGFFQD YVETGKATAE ELLTNVALTS RDNARTPFQW DDSANAGFTT GKPWLKVNPN YTEINAAREI GDPKSVYSFY RNLISIRHET PALSTGSYRD IDPSNADVYA YTRSQDGETY LVVVNFKAEP RSFTLPDGMH IAETLIESSS PAAPAAGAAS LELQPWQSGI YKVK //