ID K8ZA34_9ENTE Unreviewed; 751 AA.
AC K8ZA34;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Maltose phosphorylase / Trehalose phosphorylase {ECO:0000313|EMBL:EKU26917.1};
DE EC=2.4.1.64 {ECO:0000313|EMBL:EKU26917.1};
DE EC=2.4.1.8 {ECO:0000313|EMBL:EKU26917.1};
GN ORFNames=C683_1192 {ECO:0000313|EMBL:EKU26917.1};
OS Catellicoccus marimammalium M35/04/3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Catellicoccus.
OX NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU26917.1, ECO:0000313|Proteomes:UP000016057};
RN [1] {ECO:0000313|EMBL:EKU26917.1, ECO:0000313|Proteomes:UP000016057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU26917.1,
RC ECO:0000313|Proteomes:UP000016057};
RX PubMed=23405330;
RA Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., Santo Domingo J.W.;
RT "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT Commonly Found in Gull Feces.";
RL Genome Announc. 1:E00019-12(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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:EKU26917.1}.
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DR EMBL; AMYT01000022; EKU26917.1; -; Genomic_DNA.
DR RefSeq; WP_009492016.1; NZ_AMYT01000022.1.
DR AlphaFoldDB; K8ZA34; -.
DR STRING; 1234409.C683_1192; -.
DR PATRIC; fig|1234409.3.peg.1144; -.
DR eggNOG; COG1554; Bacteria.
DR OrthoDB; 9758855at2; -.
DR Proteomes; UP000016057; Unassembled WGS sequence.
DR GO; GO:0047656; F:alpha,alpha-trehalose phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate 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 Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 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; 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; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF14; MALTOSE PHOSPHORYLASE; 1.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:EKU26917.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016057};
KW Transferase {ECO:0000313|EMBL:EKU26917.1}.
FT DOMAIN 14..260
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 316..671
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 685..741
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 480
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 584..585
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 751 AA; 87483 MW; B20201921EC22134 CRC64;
MKRKFAVDPW KVYTTTLDKE DKRLQESITS LGNGYMGMRG NFEETYSADH HQGIYLGGVW
YPDKTRVGWW KNGYPEYFGK VINAMNFLRL QITIDGKEVD LATEQYEDFY LGLDLQHGIL
QRHYTILRGG KKITLAFERF VSLTTKELCA VNVKITSNQK AKVEIISYLD NEVTNEDANY
DEMFWQSIAK EEGGLVVQTI PNAFGIEQFT VAANMDHRVQ NLSYSGHNEE ELQVTMNFFG
EVDVDTAIEF EKRIIVTTSR DYKEKEVLAK AKEKQASLQS LSYQELKEQQ ENAWLERWKY
ADVEIEGSVE DQQGIRFNLF QLFSTYYGED ARLNIGPKGF TGEKYGGATY WDTEAYCLPL
YLALTDQKVA RNLLEYRFQQ LPQAYHNARQ QGLKGALYPM VTFTGVECHN EWEITFEEIH
RNAAMVYAIY RYTLYTGDTS YLEHEGLEVM TGVARFWADR VHYAKNKGVY MIHGVTGPNE
YENNVNNNWL TNRLAKWVLS YTKETLNTYA YRKEELGISE AELAKWTDII EHMYEPKDEE
KGIFVQHDTF LDKDLMPVSD LAKEDLPLNQ NWSWDKILRS CFIKQADVLQ GLYYFNNEFT
LEEKRRNFEF YEPMTVHESS LSPCIHAILA AELKKNEKAV ELYKRTARLD LDNYNNDTED
GLHITSMTGS WLSIVEGFAG MRTFDGLHFQ PFLPTEWKQY AFHINYRGRL LFIKVSEAGV
EVQLLEGKPM VLSIYDKEYS LENELYVPLE K
//
