ID A0ZEN3_NODSP Unreviewed; 983 AA.
AC A0ZEN3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Maltose phosphorylase / Trehalose phosphorylase {ECO:0000313|EMBL:AHJ31108.1};
DE EC=2.4.1.64 {ECO:0000313|EMBL:AHJ31108.1};
DE EC=2.4.1.8 {ECO:0000313|EMBL:AHJ31108.1};
GN ORFNames=NSP_48160 {ECO:0000313|EMBL:AHJ31108.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ31108.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ31108.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ31108.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR610972-3};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR610972-3};
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DR EMBL; CP007203; AHJ31108.1; -; Genomic_DNA.
DR RefSeq; WP_006196059.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZEN3; -.
DR STRING; 313624.NSP_48160; -.
DR PATRIC; fig|313624.11.peg.4824; -.
DR eggNOG; COG0637; Bacteria.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_0_1_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0047656; F:alpha,alpha-trehalose phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050082; F:maltose phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02598; HAD_BPGM; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR InterPro; IPR010972; Beta-phosphoglucomutase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01990; bPGM; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR NCBIfam; TIGR02009; PGMB-YQAB-SF; 1.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:AHJ31108.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Transferase {ECO:0000313|EMBL:AHJ31108.1}.
FT DOMAIN 19..259
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 311..694
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 713..741
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 770
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 772
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 770..772
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 786
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 805..810
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 813
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 835
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 873..877
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 904
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 928
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 929
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 929
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 873
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
FT SITE 904
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
SQ SEQUENCE 983 AA; 111349 MW; 25AC9E56D6908388 CRC64;
MNKKSPNNRF IYTDWILIET QFDPDELHSR ETVFTIGNGY LGTRGSFEEG YIRALPATFI
HGVYDDVPVV YTELANCPDW LPLVISINGE SPTETLRERF RLDQGEILRY DRQLDLRQGI
FSRSLRWRSP SGKTIDIHFE RFASLADQHV LGQRCQVTPV DFDGMIEIQA SINGYPENQG
FNHWEAIDQG KTAAGIWLHS RTRGSRIEIG MAARMAISGT EAALEVHTAP GYPTITATFL
ATSQQTVTVE KTVTVFTSRE VSQPVSAAQE KLAQLPDYIT LLQANAQAWN QVWHYSDILI
EGDSKAAFAV RYNLFQLLIA APKDDEKVSI PAKTLSGFGY RGHIFWDTEI FILPFFTFTQ
PVLARNLLSY RYHTLNGARR KASHYGYKGA MYAWESAVTG DEVTPRWSLP SDFYGEDIRI
WCRDHEIHIS SDISYTVWYY WQATGDDEWM QKCGAEIILD TAIFWNSRVE FNSEQDRYEI
RGVIGADEYH EFVHNNTFTN RIVQWHLEKA LIVDDWLHQN FPEQAQELEQ KLQLTAEIKT
QWSDIIAKIW IPYDAETGLI EQFEGFFQLE DVNLNDYEPR TQSMQGILGI EKTNKLQVLK
QPDVLMLLYL MRELGDFPYN QKSLQANWDY YAPRTDITYG SSLGPAIHAI LASDLGKSAE
AYERFMQAAM VDLEDVRGNA ADGIHGANAG GIWQAVVFGF GGIKLRDSRP LANPHLPQGW
TRLKFKLQWR GKWHEFDLRP QITQEESNKG FILFAPSSDH TSKIQGVIFD LDGVLTDTAE
YHYQAWQKLA DEEGIEFNRQ DNEALRGISR GASLMLMIKN RKFSESQIQE MLERKNRYYV
DLIVNITPKD VLPGAIALLD ELRQQGIKIA IGSASKNAQV VVERLGIANH VDAIADGYSV
QQPKPAPDLF LHAAQQLAVP PEQCLVFEDA AAGVEAALAA GMWAVGLGPS ERVGMAHVVL
PSLAGVKWAE LQDKLREAVA QKN
//
