ID U4KRD2_9MOLU Unreviewed; 803 AA.
AC U4KRD2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:CCV65648.1};
GN ORFNames=BN85306270 {ECO:0000313|EMBL:CCV65648.1};
OS Paracholeplasma brassicae.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Paracholeplasma.
OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV65648.1, ECO:0000313|Proteomes:UP000032737};
RN [1] {ECO:0000313|EMBL:CCV65648.1, ECO:0000313|Proteomes:UP000032737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX PubMed=24158107; DOI=10.1159/000354322;
RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT A. laidlawii and Their Comparison to the Obligate Parasites from '
RT Candidatus Phytoplasma'.";
RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
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; FO681348; CCV65648.1; -; Genomic_DNA.
DR AlphaFoldDB; U4KRD2; -.
DR STRING; 61635.BN85306270; -.
DR KEGG; abra:BN85306270; -.
DR HOGENOM; CLU_010198_1_1_14; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
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:UP000032737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 651
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 803 AA; 93390 MW; 1063BF089ACBC1F8 CRC64;
MINIFKDKKT FKEIFIDKVE STYAIDFNES NTYQQYVCLG QLLKQHIGKD WNQTRKKEKE
MRQVYYFSME FLMGRMITNN LMNAGVYDVV KETFDELGLD LNEVEHKESD AGLGNGGLGR
LAACFMDSVA ALKLPVHGNS IRYRYGFFKQ KIENGYQVEY PDRWLKDIHV WETRRQEESV
DIPFYGHIEI NVDDNGKLHV YHKNAEYVKA VPYDVPVIGY HNQVVNTLRL WSAEPSDLYE
NQGGTFEYHK KLRQISEMLY PNDETDEGKI LRLKQQYLFS AAGLNAVLRK HKEIFGTLEN
LSEKAVFHIN DTHPTLIIPE LMRVLVDEEG MDWDKAWDIT RNCVAYTNHT ILAEALEKWP
IRLFQPLLPR IYTITEEIHR RFEMELRAHF GENAREVLAM AILKDGMVHM ANLAITGSFS
VNGVAALHTD ILKEIEMKDF NDYYPNKFNN KTNGITHRRW VVQSNPELVS ILKDTIGDEW
IYDTTKLEGL LKFTNDDQIL KRYDEMKLAR KTALADKIYK EQGIQIDPTS IFDIQVKRLH
EYKRQLMNAL HIMHVYNELK TKPEVRQSFH PQTFIFGAKA APTYYFAKKV IKLINTIAEK
INNDSETSKY LKAVFVEDYN VTYAETIMPA ADLSEQISTA SKEASGTGNM KFMMNGALTI
GTLDGANVEI GELVGNDNIF IFGLDAKEVT QLQKEATYKP YDLYLNDPKI KRVIDQLTNG
FFTNVPQNEF EEIRRNLLDK DQYYILKDFD AYVKAQQKAN KAYQDRTAWL KKSMINTAKS
GFFSTDRTMF EYNRDIWHLE TIK
//
