ID E3I3Q3_RHOVT Unreviewed; 833 AA.
AC E3I3Q3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Rvan_1129 {ECO:0000313|EMBL:ADP70400.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP70400.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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 ---------------------------------------------------------------------------
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; CP002292; ADP70400.1; -; Genomic_DNA.
DR RefSeq; WP_013418804.1; NC_014664.1.
DR AlphaFoldDB; E3I3Q3; -.
DR STRING; 648757.Rvan_1129; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; rva:Rvan_1129; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_5; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000001399; 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:UP000001399};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 678
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 833 AA; 94090 MW; 3417C29A2BBF4B79 CRC64;
MTETKSQAEL RVHAAEGDER ENAQERIVEL REQILAHLIS KTGRDRSSAS TRDWFLATAL
TVRDRIVERW IDSKQESFDQ GQRRVYYLSL EFLIGRLLMD SLNNLGLTAS VREALSGLDV
DLEELREIEP DAALGNGGLG RLAACFMESM ATLSVAAYGY GIRYDHGLFR QAIKDGWQHE
YPEDWLAFGN PWEFPRPEIE YEIGFGGSVE AKADGRAAQI WKPNEIVEAV AYDTPVAGWR
GASVNTLRLW RSRAPDPLRL DVFNAGDYVA AQADQVRAES ISKVLYPSDS TPAGLELRLR
QEYFFAAASL KDLIRRHLAQ HGDITTLAEK NAIQLNDTHP AIAIAEMMRL LVDVYALEWD
EAWRITQQTF SYTNHTLLPE ALESWAVPLM ERLLPRHMQI IYLINALHLD RLRSAGHHDW
GLLSSVSLID EHSGRRVRMG TLAFLGSHKV NGVSQLHTDL MKETVFRDLH SLYPDRIVNK
TNGITFRRWL FEANPGLTRL ISETIGPAFL DDPEALRKLE AVAADKEFQA RAMSVKQKNK
EALAKIITDR LLIKVDPDAL FDVHVKRIHE YKRQLLNVLE TIACYNDIRA HPTKDFVPRV
KIFAGKAAAS YHQAKLIIKM IHDVGRVINN DPSVRGLLKV VFLPNFCVSL AERIIPASDL
SEQISTAGME ASGTGNMKFA LNGALTIGTL DGANVELRER VGDENIFIFG LTAEEVQNHR
AQGIDARATI AGSPVLKDVL DSLASGVFSH DDRDRYKQLV DILTYHDHFM VTADFDAYCE
AQRLADIRWR DRKSWWRSSI LNTARVGWFS SDRTIAEYAE DIWRVPVRTV SKS
//
