ID A0A3S2UTT6_9RHOB Unreviewed; 793 AA.
AC A0A3S2UTT6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=DXV76_11970 {ECO:0000313|EMBL:RVT84396.1};
OS Rhodobacteraceae bacterium CCMM004.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2499834 {ECO:0000313|EMBL:RVT84396.1, ECO:0000313|Proteomes:UP000287438};
RN [1] {ECO:0000313|EMBL:RVT84396.1, ECO:0000313|Proteomes:UP000287438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM004 {ECO:0000313|EMBL:RVT84396.1,
RC ECO:0000313|Proteomes:UP000287438};
RA Zhang Z.;
RT "Salalgibacter marinus gen. nov., sp. nov., isolated from a Synechococcus
RT culture.";
RL Submitted (JAN-2019) 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:RVT84396.1}.
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DR EMBL; RZWH01000003; RVT84396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2UTT6; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000287438; 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:UP000287438};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 640
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 793 AA; 88098 MW; 5B15C212A9AE9308 CRC64;
MTATAFRDDV LRHLKYTMGK DPEHAQVSDW RLALSYAVRD RIVDPWFAAT RASYDQQAKR
VYYLSMEFLI GRLLEDAIVN LGLLDEAARV MDALGVPLSE VMDDEPDAAL GNGGLGRLAA
CFLESLSSIG VPSMGYGIRY EHGLFKQGFR NGRQTEEAEA WLARPDAWAF ERPEAAFHIG
FGGDVRRSGG KTEWIPAEAV VAEAFDTPIV GWQGAWANTL RLWSARPESL FDLERFNRGD
YSGAAEPEAL ARTISRVLYP DDTTDGGKRL RLKQEFFFTA ASLRDILRRF RSEYGRDYDR
LPQKVAIQLN DTHPAIAGPE LVRLLHDEEG LDLAHAIGLA QGTLNYTNHT LLPEALERWP
VGLMADLLPR HMELIEDIDA AHAQIHPGRG VSLVEHGEAK MGELAFVMAN RVNGVSALHT
GLMKETVFKD LHALHPERIV NQTNGVTPRR WVLSANPRLS ALITEAIGDG WVGDLEQLSE
LEPFVDDAGF VERYAQAKAQ NKADLAQFLR EDRGLVLDPD AMFDVQIKRI HEYKRQHLNI
LETVALWQEI HDDPQGDWTP RVKIFGGKAA PGYVFAKEII HLINSVAARL NDDPVTSKYL
RVAYPANYNV SLAERLIPAA DLSEQISTAG KEASGTGNMK FALNGALTIG TLDGANVEIR
ERVGEEHFFL FGMTADEVTA RRRIAGHAAQ AIAADPRLQR ALAAVRDDTF APGEPGRFAG
IADNIAGPDY FLVASDFTDY WRAQREVDAA YRDPSGWMKS ALLNTARSGW FSSDRTIRGY
MADIWDARPV AAE
//
