ID A0A2M8IXS4_9RHOB Unreviewed; 783 AA.
AC A0A2M8IXS4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CVM52_17680 {ECO:0000313|EMBL:PJE35339.1};
OS Pseudooceanicola lipolyticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=2029104 {ECO:0000313|EMBL:PJE35339.1, ECO:0000313|Proteomes:UP000231553};
RN [1] {ECO:0000313|EMBL:PJE35339.1, ECO:0000313|Proteomes:UP000231553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=157 {ECO:0000313|EMBL:PJE35339.1,
RC ECO:0000313|Proteomes:UP000231553};
RX PubMed=29219804; DOI=10.1099/ijsem.0.002521;
RA Huang M.-M., Guo L.-L., Wu Y.-H., Lai Q.-L., Shao Z.-Z., Wang C.-S., Wu M.,
RA Xu X.-W.;
RT "Pseudooceanicola lipolyticus sp. nov., a marine alphaproteobacterium,
RT reclassification of Oceanicola flagellatus as Pseudooceanicola flagellatus
RT comb. nov. and emended description of the genus Pseudooceanicola.";
RL Int. J. Syst. Evol. Microbiol. 68:409-415(2018).
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:PJE35339.1}.
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; PGTB01000098; PJE35339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8IXS4; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000231553; 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:UP000231553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 632
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 783 AA; 87613 MW; 5CC5E85A930E52C3 CRC64;
MKDAIGRHLS YSIGKTPGAA TLRDWRMAVS LAIRDRMADA WFASTRRTYE AGAKRVYYLS
MEFLVGRLLE DGIVNLRLEE RVSEALAELG QDYAEVIADE PDAALGNGGL GRLAACYLES
MSTLGCPAYG YGIRYEHGLF RQQIVDGRQV ERPETWLQQP HAWEFERPES RYEIGFGGSV
RDGTVWTPGE SVWAEAFDTP VAGWNGRWVN TLRLWSAKPT EPFDLDRFNR GEYAAAAESE
ALARTISRVL YPDDTTEQGK ELRLKQEYFF SAASIRDILR RFESQFSDLR QLPEKVAIQL
NDTHPAIAGP ELVRLLCDEK GLDFDEALQI AQGTLNYTNH TLLPEALEHW PEGLFGRLLP
RHLAIIDRID HAHAKANPSR TSSVRDHGQV KMGELSFIMA NRVNGVSALH TELMKSTVFA
ELHRLHPERI VNQTNGVTPR RWLLSCNRRL STLIEERLGL GWVDDLEQLH DLEPHLDDPA
FLDAYAAAKT ANKADLADWM NRTQEGLTAD PAMMFDVQIK RIHEYKRQHL NILETIALWQ
AMRDAPNAGW TPRLKLFAGK AAPGYVFAKE IIHLINAVAK VVNADKITNK MLQVAFLPNY
NVSLAEKLIP AADLSEQIST AGKEASGTGN MKFALNGALT IGTLDGANVE IRDRVGAENF
FLFGMTTDEV DQRRAIPDHA AKAVEADSRL ARALAAVRDG RFSPEDPGLF RGIADNISGP
DYFLVASDFS DYWRAQREVD GAFANAGDWT RRAALNTARS GWFSSDRAIR GYLDDIWGAE
TLL
//
