ID A0A0W1KK81_9ACTO Unreviewed; 788 AA.
AC A0A0W1KK81;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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 Name=malP {ECO:0000313|EMBL:KTF04401.1};
GN ORFNames=AQZ59_00923 {ECO:0000313|EMBL:KTF04401.1};
OS Trueperella bernardiae.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF04401.1, ECO:0000313|Proteomes:UP000054404};
RN [1] {ECO:0000313|EMBL:KTF04401.1, ECO:0000313|Proteomes:UP000054404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF04401.1,
RC ECO:0000313|Proteomes:UP000054404};
RA Bernier A.-M., Bernard K.;
RT "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT 0504T, Isolated from Blood Culture.";
RL Submitted (NOV-2015) 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:KTF04401.1}.
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DR EMBL; LNIZ01000003; KTF04401.1; -; Genomic_DNA.
DR RefSeq; WP_062613483.1; NZ_LNIZ01000003.1.
DR AlphaFoldDB; A0A0W1KK81; -.
DR STRING; 59561.AQZ59_00923; -.
DR PATRIC; fig|59561.3.peg.915; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000054404; 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:UP000054404};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 632
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 788 AA; 89371 MW; E67F09E919481942 CRC64;
MTHDNLTATI AGQVRSVSGK NVLSATLQEY WQGTAAAVVD HLADNWQKTE ERYNASRMQH
YFSAEFLMGR ALLNNLNNLG LVEEAEQALG AFGQNLSDVL EEEHDAALGN GGLGRLAACF
LDSSATQNLP VRGYGILYRY GLFKQFFEDG NQGEEPDPWM EEGYPFVIRR EENVKFINYA
DLKVRAIPYD MPITGYGTDN VGTLRLWKAE PMADFDYNAF NSQDFTGAIV ERERVNDISR
VLYPNDSSFE GKVLRVRQQY FFCSASLQQI VDNELAQRGT LKDFATFNSI QLNDTHPVLA
IPELMRILMD DHDFGWDEAW EIVRGTFAYT NHTVLAEALE TWEVSIFDRL FPRIREIIFE
IDRRFREEIA KAGFDQGKID YMAPVSGNRI RMAWIACYAA FSINGVAALH TEIIKADTLK
DWYDVWPEKF NNKTNGVTPR RWLDQCNPRL SALLTELLGN DEWVRDLDLL KNLEGYLNDA
DVLDRLNAIK HANKVDFAAW IKHRQGIEVD PDAIFDTQIK RLHEYKRQLL NAFYILDLYF
QIKDDPSMEV PPRVFIFGAK AAPGYVRAKA IIKLINTIGE LVNNDDDVAG RLKVVFVENY
NVSPAEHIIP ATDISEQIST AGKEASGTGN MKFMMNGALT LGTMDGANVE IVDAVGNDNA
YIFGATEDEL PELRKTYDPR RTAAEVPGLQ RVMDALVDGT LDDGGTGLFH DLHNSLFDGW
GGADEYYVLG DFASYRETRD RVAADYFSDR RHWAAMCLKN IIESGRFSSD RTIRDYAREV
WKIEPQKI
//
