ID F6DLN0_DESRL Unreviewed; 850 AA.
AC F6DLN0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:AEG61672.1};
DE EC=2.4.1.1 {ECO:0000313|EMBL:AEG61672.1};
GN OrderedLocusNames=Desru_3469 {ECO:0000313|EMBL:AEG61672.1};
OS Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
OS (Desulfotomaculum ruminis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG61672.1, ECO:0000313|Proteomes:UP000009234};
RN [1] {ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., Plugge C.M., Muyzer G.,
RA Kuever J., Parshina S.N., Ivanova A.E., Nazina T.N., Brambilla E.,
RA Spring S., Klenk H.-P., Woyke T.;
RT "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG61672.1, ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RX PubMed=23408247; DOI=10.4056/sigs.3226659;
RA Spring S., Visser M., Lu M., Copeland A., Lapidus A., Lucas S., Cheng J.F.,
RA Han C., Tapia R., Goodwin L.A., Pitluck S., Ivanova N., Land M., Hauser L.,
RA Larimer F., Rohde M., Goker M., Detter J.C., Kyrpides N.C., Woyke T.,
RA Schaap P.J., Plugge C.M., Muyzer G., Kuever J., Pereira I.A.,
RA Parshina S.N., Bernier-Latmani R., Stams A.J., Klenk H.P.;
RT "Complete genome sequence of the sulfate-reducing firmicute
RT Desulfotomaculum ruminis type strain (DL(T)).";
RL Stand. Genomic Sci. 7:304-319(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; CP002780; AEG61672.1; -; Genomic_DNA.
DR RefSeq; WP_013843418.1; NC_015589.1.
DR AlphaFoldDB; F6DLN0; -.
DR STRING; 696281.Desru_3469; -.
DR KEGG; dru:Desru_3469; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000009234; 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; 2.
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:AEG61672.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009234};
KW Transferase {ECO:0000313|EMBL:AEG61672.1}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 602
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 850 AA; 99048 MW; 098107F6A673A4E1 CRC64;
MYSFRTISVM PEMPERISRL TELARNLWFS WRPRSQQLFS KIDRVLWEEV NHNPVKFLLH
VDKGKLEKAA DDPNYLYMYD LMMGYLDEYM KKETWYQKKF PDQANQLIAY FSAEFGVHES
NPVYSGGLGL LAGDHCKSAS DLGLPFVGVG ILYKQGYFYQ RINREGWQEA HYSFMDFNEM
TVTPASKNGG DVIVTVPLPG RDLFVKVWEL QVGRITIYFL DADLAQNRME DRLLTSTLYG
GDQATRISQE IILGIGGVKA LRELGISPTA WHINEGHASF SIVERIRELV EKEIPFAVAS
EAVRSCTIFT THTPVPAGHD VFSPEMIDQY LSYFYDKLHV SRDVFMGMGW DDRRQGFNMT
KLAMNHSVFT NGVSKLHGEV TKKMFAYQYT GIPMEEIPIY YVTNGVHTET WADREMKQLF
EKYIGMNWME NISNQEQWQR VYDISDEELW QVHMLLKERM IQFVQHNLCR RMERNFEPIE
LIRENAGYLS KDVLTIGFAR RFATYKRANL LLRNKDRLAR LLNNPERPVQ IIFSGKAHPA
DRPGQEIIKQ LLDLAEEERF RGKIVFVENY DINVSRHLLQ GVDVWLNTPR RPLEASGTSG
QKAAVSGIIN CSIMDGWWPE AYNGENGFAI GSELEYDNEE IQDREDANSL FDLLEQTIVP
YYYRRVNGIP REWVRRMKNS LATIPWRFST ERMVKEYTQR FYLPAAMKGR RYMAQEYKVA
QQMQEHKRYM QENWHHVHFQ SIRVDQPKTL KVGQNIFIQA DVCLGSIKPQ DVIVEVVYGK
VGDKALVDVM LMPMNLKEPV GQDLYRYETN LVLLQGTSGY TLRVRPYSPN FEYPFELPLI
KWGDNMSFST
//
