ID R7GPW3_9FIRM Unreviewed; 798 AA.
AC R7GPW3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BN591_01406 {ECO:0000313|EMBL:CDE29086.1};
OS Catenibacterium sp. CAG:290.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Catenibacterium; environmental samples.
OX NCBI_TaxID=1262767 {ECO:0000313|EMBL:CDE29086.1, ECO:0000313|Proteomes:UP000018308};
RN [1] {ECO:0000313|EMBL:CDE29086.1, ECO:0000313|Proteomes:UP000018308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:290 {ECO:0000313|Proteomes:UP000018308};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDE29086.1}.
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DR EMBL; CBIQ010000158; CDE29086.1; -; Genomic_DNA.
DR AlphaFoldDB; R7GPW3; -.
DR STRING; 1262767.BN591_01406; -.
DR Proteomes; UP000018308; Unassembled WGS sequence.
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:UP000018308};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 645
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 798 AA; 92393 MW; F3234C769AD039E1 CRC64;
MFNTKEEFKY EFSKRIIESY GRTVEEAHLT EKFMVLETMV RDYASVNWAM TKMAVQAKQQ
KQVHYFSMEF LVGRLLVNNM MNLGIYETAK EGLADYGINI HDLEELESDA GLGNGGLGRL
AACFMDSLAS LSYPAFGNTI RYDYGFFKQK IENGYQVEVP DQWLRLGNMW EVRKPKHATE
VKFWGKVIWD DATGGWKHVD YEAVRAVPYD MPIVGNDTKV TNTLRLWKAE PSENIPTNKD
FRQYAQEVND ICQTLYPDDS THAGRVLRLK QQYFFVCAGL NSIIRAHLRV YPDLTNFHEK
NVIQLNDTHP VLVIPELMRV FIDDYNMEWD DAWNIVCKTC AYTNHTILAE ALEKWPVDMM
RDLLPRVYQI IEEINRRFIG FVKQQTENDN ELLQRVMIIK DGQVHMARLA IAGSFSVNGV
AQLHSDILKE REMKDFDTLY PNKFNNKTNG VTHRRWLAYC NPQLTSLINE SIGDSWMHRP
DDLEKLAPYV TDSITQSKFY NVKQQRKQIL ADYIKEHNGI DVDVNSIFNI QVKRLHAYKR
QLLNVMHIIY LYQRMKEDSS FRIYPHTYIF GAKAAPSYYL AKKIIKLINS VAEKVNNDPE
TNKYLKVVFI ENYGVTIAEK IIPAADVSEQ ISTAGKEASG TSNMKFMMNG ALTLGTLDGA
NVEIAELVGD DNIVIFGMKD NEVNDLKASG SYSSWNEYNN NPNIKKVIDS LVDGTWNTSR
EEFKIIFDEL MARNDEYFLL KDFESYRLAQ EKINNLYQDR ANWSKICLAN IAKSGHFSSD
RTIEDYVKDI WHLNRVKI
//
