ID C7LTW8_DESBD Unreviewed; 816 AA.
AC C7LTW8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Dbac_1498 {ECO:0000313|EMBL:ACU89591.1};
OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS (Desulfovibrio baculatus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU89591.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU89591.1, ECO:0000313|Proteomes:UP000002216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX PubMed=21304634; DOI=10.4056/sigs.13134;
RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL Stand. Genomic Sci. 1:29-37(2009).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC carbohydrate metabolism. Enzymes from different sources differ in their
CC regulatory mechanisms and in their natural substrates. However, all
CC known phosphorylases share catalytic and structural properties.
CC {ECO:0000256|ARBA:ARBA00025174}.
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 ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; CP001629; ACU89591.1; -; Genomic_DNA.
DR RefSeq; WP_015773682.1; NC_013173.1.
DR AlphaFoldDB; C7LTW8; -.
DR STRING; 525897.Dbac_1498; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; dba:Dbac_1498; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_7; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000002216; 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:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002216};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 664
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 816 AA; 93163 MW; BDC5956ABB833160 CRC64;
MANPEINEIV ESLKDDIQRH VALTLGSDPF PPRKGRYYLG LCYSVRDRLL GQWIETQRSY
YDSITKRVYY MSLEFLPGRF LMNYIQALGL EEVCREAVRD FGLDLDELLE EEWNPGLGNG
GLGRLASCYM DSMATCKIPG YGYGILYDYG IFYQTIVNGY QHEGCDNWLR QDSPWVLRRG
HFMFRINFYG RSEAYEDSAG HERFRWVDTE SVMAMACDIM VPGHQNGHVT NMRLWKAIST
RDFELEHFNR GDYIGAVQAK VESENISKVL YPNDTSPRGK ELRLRQQYFF VAATFQDILR
RFRKNNYSSF DCFPDQVAVQ LNDTHPAISI AELMRILVDE EALTWESAWS ICQKTFSYTN
HTVLPEALET WSVELIGRML PRHLQIIFEI NHRFLDDVGK RFPGRVDLLR SLSLVAEGDG
KQVRMAHLAI VGSHTVNGVA ELHSQILKTR LFKDFNALYP GKFTNVTNGI TPRRWLMQAN
PSLAELITSV IGDEWIHDLS HLSELAAHAD DPEFQQRWQE VRKRNKKLLA RYVLRKLGVG
INPATLFDMH IKRIHEYKRQ ILNVLHVITL YNRIRSESLE HHVPRTVFFA GKAAPGYFQA
KLIIKLINSV AQAVNGDSAV GNDLRVVFLP NYCVSQAEKL IPAADLSEQI STAGMEASGT
GNMKFALNGA LTIGTLDGAN IEIREVVGED NFFLFGHTES DVHRLHSGGY DPVQIYESNI
ELKKALDMIS TGFFSPEAPD LFRPIVDSLL AHGDYYLVLA DYAKYVAEQG NVSKCYEDRP
LWTRMSILNT ANMGKFSSDR SIMEYARNIW NVSPLA
//
