ID D3RQ12_ALLVD Unreviewed; 834 AA.
AC D3RQ12;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Alvin_2714 {ECO:0000313|EMBL:ADC63623.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC63623.1, ECO:0000313|Proteomes:UP000001441};
RN [1] {ECO:0000313|EMBL:ADC63623.1, ECO:0000313|Proteomes:UP000001441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC {ECO:0000313|Proteomes:UP000001441};
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(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}.
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DR EMBL; CP001896; ADC63623.1; -; Genomic_DNA.
DR RefSeq; WP_012971891.1; NC_013851.1.
DR AlphaFoldDB; D3RQ12; -.
DR STRING; 572477.Alvin_2714; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; alv:Alvin_2714; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_6; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000001441; 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:UP000001441};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 680
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 834 AA; 95025 MW; 01E080E417226EBC CRC64;
MSSSTKLIQN CPNESTFDLP PLSLDPEGIA HDFRHYYVHT FGRDRDCLSA YYPYRALATT
LRDRLMERWK TTRQAYDKTG CKRAYYLSLE FLMGRALSNA TFNLDLDEAV ARGLHTLGLE
LEEIASTEPD PGLGNGGLGR LAACFLDSCA TLQLPVRGYG LRYEYGMFRQ TIENGAQVEE
PDHWLREGNP WEIERPEFTQ RIQFGGHTET HRDQNGRIVV SWVDTHDVLA VPYDVPVPGY
RNDTVNTLRL WKAAATDEFD LDEFNAGSYT ESVAQKNAAE HITMVLYPND ASENGKELRL
RQQYFLASAS LKDVLRDWIR LHGQDFSRFA DLNCFQLNDT HPAVSVAELM RQLMDEHHLE
WHDAWDITRR TMAYTNHTLL PEALERWPVR LFRQLLPRIL EIIFEINARF LAEVALRWPG
DVDRQRRMSL IEEGHDPQVR MAYLAIVGSF SVNGVAALHS QLLVEGLFRD FHELWPEKFN
NKTNGVTPRR WLAMCNPGLR DLLDETIGTG WTRDLEQLSR LAPYAEDAAF RARWHAIKQA
NKARLVEQIA GICKVEFPLE AMFDVQVKRI HEYKRQLLNV LHVIHLYNRI KRGDTANWTP
RCVLIGGKAA PGYFMAKQII KLINHVARVV NMDPATAGLL RVAFVPDYRV SLMEVIAPGT
DLSEQISTAG KEASGTGNMK FMMNGAVTIG TLDGANIEIR EQVGADNFFL FGLTAAGVES
LRGHYDPNAI IASDPALWDV MNLLESGHFN QFENGVFDSV ILSIRNPHDP WMTAADFRSY
VEAQERAAAA YRDREHWLRM SILNSAHSGR FSSDRTIAEY NSDIWHLETV APKR
//
