ID A0A0B5DWJ6_9RHOB Unreviewed; 775 AA.
AC A0A0B5DWJ6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=P73_3068 {ECO:0000313|EMBL:AJE47783.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE47783.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE47783.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE47783.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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; CP004393; AJE47783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5DWJ6; -.
DR STRING; 1208324.P73_3068; -.
DR KEGG; cid:P73_3068; -.
DR HOGENOM; CLU_010198_1_1_5; -.
DR Proteomes; UP000031521; 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:UP000031521};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 622
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 775 AA; 87875 MW; FF912529E471BCD5 CRC64;
MGKDPEHAKF FDWRMALSHA IRDRIVDRWV ASTRRTYEQD GKRVYYLSME FLIGRLLEDG
IVNLGLVEEV GETLRTFGID YRSVLEDEPD AALGNGGLGR LAACFLDSLS TIGCPAMGYG
IRYENGLFKQ SFVDGRQVES PETWLQEPHP WEFGRPEVRF TLGFRGEVTT ENGRTVWKPS
ELLQAEAFDT PIVGWQGRWA NTLRLWAGRA VDPFDLDRFN AGDFAAAAEH EALARTISRV
LYPEDSNEAG KELRLKQEFF FSAASIRDIL RRFEGQHEDL RALPKKVAIQ LNDTHPAIAG
PELLRILHDE RGLSFEEALE ITHGCMNYTN HTLLPEALER WDERLFGRLL PRHLQIIDRI
DDAHYRANPT RLLSARSDGQ VKMGELSFIV ANKVNGVSAL HTDLMKKTVF KDLHGLHPDR
IVNETNGVTP RRWLHSCNPG LSSLITDSIG DGWIADLEQL ERLEPFIGKD DWLHRFRAVK
AENKVTLCDY IAERHGMRLN PDAMFDIQIK RIHEYKRQHL NILEAIAHWQ EIKDTPGGDW
VPRVKIFAGK AAQGYHFAKD IIHLINDVAK VVNADAETRD SLQVIFLPNY NVTLAEHLIP
AADLSEQIST AGKEASGTGN MKFALNGALT IGTLDGANVE IRERVGEENF FLFGMLADEV
MQRRMIHDHA QQAIAADPRL ARALEAIRSG TFSPQDPGRY VHIADNLTWS DYFLVCSDFS
AYWQAQREAD HAYRDPDLWA RKAALNVARS GWFSSDRTIR GYMCDIWGAE SLLAP
//
