ID B0VG65_CLOAI Unreviewed; 825 AA.
AC B0VG65;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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:CAO80283.1};
GN OrderedLocusNames=CLOAM0378 {ECO:0000313|EMBL:CAO80283.1};
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO80283.1, ECO:0000313|Proteomes:UP000002019};
RN [1] {ECO:0000313|EMBL:CAO80283.1, ECO:0000313|Proteomes:UP000002019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX PubMed=18245282; DOI=10.1128/JB.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(2008).
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; CU466930; CAO80283.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VG65; -.
DR STRING; 459349.CLOAM0378; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; caci:CLOAM0378; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_0; -.
DR Proteomes; UP000002019; 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:UP000002019};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 677
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 825 AA; 95205 MW; 20BD48F49ACC62EF CRC64;
MTQGEEKIMN KAFCEKLSHL SIEGTAEEIV HRFIEHLKFD LGKDEFSATP YDCYVSFASA
VKDILMDRWL ITQPQEYALQ RKRVYYLSLE YLIGRSLGNA ILNLDIQKQS IKALTENGFD
LSLLSELEWD AGLGNGGLGR LAACFLDSMA TLKIPAYGYG IRYEYGIFFQ HIINGEQVET
PDNWLRYGSV WEIARPARLF PVYFGGIVKE EILEDGSKKM RWIPEETVMA MAYDYLVPGF
QNNYVNTLRL WSAKSTREFN LAYFNEGDYM QAVADKNHSE MIAKVLYPND NKMQGKELRF
RQEYFFVSAT LQDILRRFLK KESDLRKLPE KAAIQLNDTH PAIAVAELMR ILVDERNLPW
EIAWEITQQC MAFTNHTILP EALEKWQVLL FEKLLPRHLQ IIYEINERFL SSIRITGLYD
DDFISRVSLI EEEPVKSIRM ANLAIVGSHS VNGVSELHTD ILKHLIFKDF YALWKDKFNS
KTNGITPRRW LMLCNPLLSE LITQAIGSAW KTDLKELAKL NKYKNDSTFL EDLGEVKRQN
KLEFCKYYED LHKRKLNPES IFDFQAKRIH EYKRQHLNAL GIIHLINQIR DGKTPYPQSF
FFAGKAAPGY FIAKLIIRFI CALSDYIEKD KELSRYLSVI FLPNYRVTLA ERIMPPAEIS
RQISLAGTEA SGTGNMKFAL NGALTIGTLD GANIEIREAV GEENFFLFGM TAAEVKNLKE
SGYHPYEMMR QNEDIKRIFD FIESDILNPL NPGLFTPLTD LLLYQGDKYC LIADLPDFIR
VNAEAVKVYQ DKQQWNRMSL ANIANMGKFS SDETIKGYAK DIWGV
//
