ID F0RMH0_DEIPM Unreviewed; 839 AA.
AC F0RMH0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:ADY26020.1};
DE EC=2.4.1.1 {ECO:0000313|EMBL:ADY26020.1};
GN OrderedLocusNames=Deipr_0864 {ECO:0000313|EMBL:ADY26020.1};
OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY26020.1, ECO:0000313|Proteomes:UP000007718};
RN [1] {ECO:0000313|Proteomes:UP000007718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT 20540.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADY26020.1, ECO:0000313|Proteomes:UP000007718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RX PubMed=22768367; DOI=10.4056/sigs.2756060;
RA Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the orange-red pigmented, radioresistant
RT Deinococcus proteolyticus type strain (MRP(T)).";
RL Stand. Genomic Sci. 6:240-250(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001275};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; CP002536; ADY26020.1; -; Genomic_DNA.
DR RefSeq; WP_013614629.1; NC_015161.1.
DR AlphaFoldDB; F0RMH0; -.
DR STRING; 693977.Deipr_0864; -.
DR KEGG; dpt:Deipr_0864; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_0; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000007718; Chromosome.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:ADY26020.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007718};
KW Transferase {ECO:0000313|EMBL:ADY26020.1}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 606
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 839 AA; 94950 MW; D6FF437FFC986848 CRC64;
MNILGKVTVL PKLPAAIGRL SELAYNLYWS WEPRACSLYR DLNPDIWETY GHNPVRTLLE
VGSEDMDRAA TDPEFVRRYG EVMAEFDAYM GKQDTWASRH AADLKPVAYF SMEYALHESL
PIYSGGLGVL AGDHCKSASD LGLPFTPVGL LFHDGYFRQT LGRDGWQEEK YDRLDLTTLP
IRPIRTPEHD ELRISLEIGG RTVTARVWQL NVGRIRMLLL DTDVPENHPD DRLLTSRLYG
GDQEMRLKQY MLLGIGGVRA LRAAGAPAEV WHMNEGHAGL LNLERIRERV EQGLDFRTAH
ELTAGSTLFT THTPVPAGND AFSWDLMDRY LGSWPAQLHT TREHLYSLAR SEAMEDHGPA
FNMTVFSLRM SRMANGVSKL HGQVSRDMWK HLYPGLYPEE VPIGHVTNGA HNLSFTSQRM
RDLLSTVMPE DWTERLHEPE IWQNVEQLSG AQLAGVQREM KAEMIAFVRH HQREMLLRNG
AGAAELAYTD TLLSPDVLTI GFARRFATYK RATLLLRDRE RLSRIVNHPE RPVQFVFAGK
AHPADNPGKA LIQEIYRVSQ LPEFRGKIVI LENYDMHVAR RLVQGVDVWM NNPRRPLEAS
GTSGMKASFN GSPNFSVLDG WWVEGHLEGN ANGWPIGEER EYADQAVQDD ADAFSLYQTL
EQTIVPLYYG ERGGEADSWA GVVRSAIESV SARFSMQRQV IDYVQCYYLP LSARRNLLVP
GGGQRARELA EWKAWIANQW PQVSVAASHH LPATAEPGEQ VQITAQVNPG RIAAEELRAE
VVLRRGHRVE RVPMQRREDG EYAATVALER SGMYEVGVRL YPYLPDLSHD FELGLVKWA
//
