ID F6DQI3_DESRL Unreviewed; 847 AA.
AC F6DQI3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:AEG60877.1};
DE EC=2.4.1.1 {ECO:0000313|EMBL:AEG60877.1};
GN OrderedLocusNames=Desru_2651 {ECO:0000313|EMBL:AEG60877.1};
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:AEG60877.1, 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:AEG60877.1, 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; AEG60877.1; -; Genomic_DNA.
DR RefSeq; WP_013842633.1; NC_015589.1.
DR AlphaFoldDB; F6DQI3; -.
DR STRING; 696281.Desru_2651; -.
DR KEGG; dru:Desru_2651; -.
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; 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:AEG60877.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009234};
KW Transferase {ECO:0000313|EMBL:AEG60877.1}.
FT DOMAIN 13..121
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 603
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 847 AA; 97020 MW; D50D25A2FB4205ED CRC64;
MYFFKTITVN PVLPERIGRL KELSYNLWFS WHPEALELFK QIDEQKWKEC NHNPVKLLLE
ATGADLERVA GNQDYLQLYD KVMADLDRYM TEGSWFLSKY PHLSNKSIAY FSAEFGLHES
LPIYSGGLGV LAGDHCKAAS DIGLPLVGIG LLYKQGYFTQ HINREGWQEA LYPYQNYHEM
PVKPAKSLDG REIIIPVNLP GRQIYLKVWE VQVGRIKIYL LDADITLNSD QDRKLTAQLY
GGDKDTRISQ EILLGVGGVK ALRIMGINPG AWHINEGHAA FLCIERLQEL VQTGVPLAAA
KEVVRASTLF TTHTPVSAGH DVFDADKVDY YLNRYYSLLG LDRDGFMELG WDPGRQIFNM
TILAMNLSAY CNGVSKLHGE VTRKMFHYLY EHIPVEEVPV FSVTNGIHTL TWMSEELKTL
LDAYLPSGWQ NNISDREQWE AVENIPDEEL WTLHRRLKKK CIHLVRGILK EQKERHQESV
EMLGEVEQHL NPDAFTIGFA RRFATYKRAA LLLRDKERLA RLLTDPERPV QIIFSGKAHP
ADHPGQELIK QIHDLSQQEP FKGKIVFIEN YDMNVSRHLT QGVDLWLNTP RWPMEASGTS
GMKAAANGVV NCSVLDGWWP EGYDEENGYA IGEETGYRNE EEQDRDDAYR LYSLLEEKII
PTYYHQTEGC PKEWVARMKK SIKTITPLFS TERMVKEYAE RFYTESSIRG QKFTAENFKI
ASQVHNYKRF IKENWHYVTV KGVEAPGDSE MRVGDTLQLA VKVYLGPIPP EDVKVEAVHG
CEGDHSLTSI KTVPLEVEEQ FSEGLYKYKG AFALEQGTCG FTVRIRPEHP YFATKFELPL
ASWAQSF
//
