ID R5CYC5_9FIRM Unreviewed; 664 AA.
AC R5CYC5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BN705_00685 {ECO:0000313|EMBL:CCX71509.1};
OS Firmicutes bacterium CAG:555.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263030 {ECO:0000313|EMBL:CCX71509.1, ECO:0000313|Proteomes:UP000018402};
RN [1] {ECO:0000313|EMBL:CCX71509.1, ECO:0000313|Proteomes:UP000018402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:555 {ECO:0000313|Proteomes:UP000018402};
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 -!- 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|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:CCX71509.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAWW010000062; CCX71509.1; -; Genomic_DNA.
DR AlphaFoldDB; R5CYC5; -.
DR STRING; 1263030.BN705_00685; -.
DR Proteomes; UP000018402; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000018402};
KW Transferase {ECO:0000256|RuleBase:RU000587}.
FT REGION 630..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 75714 MW; 2300BD36B92EEF55 CRC64;
MYKSQISRDE VRSAIEDKLC AQFGVTSKNA TDDQVFRASA IVIREIMSRL LALGEDRKPD
REVHYLSMEF LMGRSLMKNA FNLGISEALI GALGDLGRNA SDIFEEENDA GLGNGGLGRL
AACYMDSMAS LGIPATGYSI CYELGIFRQK IRDGKQTEVA DDWRSAAESW LVTRSDEAVE
VRFGGHIVPH WDNYGHYHAE HIGYTTVTAV PRDMLIAGYK GETVNTLRLW DARSTTALDM
YLFSEGEYVK SLEQRTMSEV ITKVLYPADD HIQGKQLRLK QQYFFVSATV QCIVRKHMER
YGDIRSFAEH HVIQINDTHP TLVIPELMRI FMDEYGLGWD EAWRIVTNAV AYTNHTVMSE
ALEKWPQELI QTLLPRVWEI LCEINRRWCE YLRSQFGESE KVGRNLIIQD DGVHMANLCL
AACFKINGVS ALHGEILKTE LFRDVCSLTP ERFTYVTNGI DHRRWLAQIN PRLNSLVCDL
LGSESYLQKP ETLIRLADFA DDTAVRDRVN EIKLLNKQDF AAFARKQDGF VLNTDAILDV
QVKRLHEYKR QLMCAMLITR LQNLLHEQPD IDFTPRTFVF GAKAAAGYYT AKRIIELILS
LADDVNHDPK CKGKLQVYFM ENYRVSAAEA LMPAAPPPQT RPPPERRSER RYPPPARRPP
ARAT
//
