ID A0A1M6XTW0_9FIRM Unreviewed; 777 AA.
AC A0A1M6XTW0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SAMN02745136_04064 {ECO:0000313|EMBL:SHL09384.1};
OS Anaerocolumna jejuensis DSM 15929.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1121322 {ECO:0000313|EMBL:SHL09384.1, ECO:0000313|Proteomes:UP000184386};
RN [1] {ECO:0000313|EMBL:SHL09384.1, ECO:0000313|Proteomes:UP000184386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15929 {ECO:0000313|EMBL:SHL09384.1,
RC ECO:0000313|Proteomes:UP000184386};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRAC01000023; SHL09384.1; -; Genomic_DNA.
DR RefSeq; WP_073278690.1; NZ_FRAC01000023.1.
DR AlphaFoldDB; A0A1M6XTW0; -.
DR STRING; 1121322.SAMN02745136_04064; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000184386; 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:UP000184386};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 626
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 777 AA; 89757 MW; 8D0F77CA40CA4112 CRC64;
MENFKQYVST ILELDYRKTI KEADTTELYH AVSKAVMQMI KKDWDKDAGS KKVSYLSAEF
LVGRLVYSNL LNSGLYHTYA EMMGENNLDI GIFEDIEDAA LGNGGLGRLA ACFLDSGATL
GIPLNGYGIR YRYGLFKQYF EDGFQREMPD DWQRFGDPWS VRKDKEKIRI DFKNQSVYAV
PYDTPVIGYG GNTVNYLRLW QAEPIEEFDF ELFNEQKYEK AVKNRDEAEA ISSLLYPNDS
TDAGKKLRLK QQYFFAAASI RDMVKRYKEK YGDDFSHFQD EYAIQLNDTH PVVAIPEFVR
ILMEEEKLSF ARAFRITRET FAYTNHTVMA EALEKWSISL FRSVIPGVYK YVQLLQKALI
KELKTFGKTA EAEQRIYNII DGNLIYMARL AVFASHSTNG VAGLHTEILK KDVLKEWYEI
YPERFQNKTN GITQRRWLSL SNMELSGFIT DRIGNSWILN LDSLKKLEEF KDNKQVIKQF
ADIKHIKKQQ LADYIKKQEN IQINPDFIFD IQVKRLHEYK RQLLNAFSIM DIYFGIKDGS
IKDFTPTLFL FGAKAAPGYF RAKGIIKYIN EIAKLINSDP EVKDLMQVVF VSNYNVSYAQ
KLVPAADISE QISTAGTEAS GTGNMKFMLN GAVTLGTYDG ANIEIVEQAG EENNYIFGAR
VEDIEAVKNT YNPAKIYQAN PRIKRVLDTL IDGTFEDNGT GMFKELYSAI LEGASWHKPD
HYYLLLDFDD YTDTRLRVNR EYKDTFHFHR KCFINTANAG LFSSDRTIKE YYNEIWK
//
