ID A0A0F0LKH9_9MICO Unreviewed; 841 AA.
AC A0A0F0LKH9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KJL32785.1};
GN ORFNames=RL72_00137 {ECO:0000313|EMBL:KJL32785.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL32785.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL32785.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL32785.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL32785.1}.
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; JYIT01000037; KJL32785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0LKH9; -.
DR PATRIC; fig|582680.7.peg.152; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000033448; 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:SF25; MALTODEXTRIN 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:UP000033448};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 690
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 841 AA; 93414 MW; 1847EA37489A279B CRC64;
MTTADAPHPH DAAAPHPEGA THPLALAPVT PPPATVDGFV AEFLRTLNFD CGVALSASTA
NDRYVALAHT VRDYLMGRWL EDLRQQKETQ AKSVCYLSAE YLLGRQLDNN LLASGLTEIA
AEALAACGLS LDELREHEIE PGLGNGGLGR LAACFIDSLA TLGVPSIGYG IRYEYGIFRQ
TFEDGQQVEQ PDAWLTLGSP WEFPHPERAQ LVSFGGRTET YDDGGVTRTR WVPAWNVSAI
PCNYMVPGFE NGRVNTLRLW RAKATDAFDL RIFNSGDYEE AVRAQTFAEN ISKVLYPEDS
TPQGKELRLQ QQYFFVAASI HDFLDTMLAE GYDLAKLGDR VIFQLNDTHP VIAVPELMRV
LVDERGMDWD AAWAVTRRCF AYTCHTLLPE ALEVWSVDLL GRLLPRHLEI IYRINEEFLA
AVRARFGDDE LRIRNMSIIA EFPERAVRMA YLATVAGSKV NGVAELHSQL LREKVLPDFD
AFYPGKFTNV TNGVTPRRFL RLANPALSSL ITEAIGEGWV TDLERLRELE PFADDAGFRA
SFAEVKAANK RRLNDVLHAR DGMRVGDGHL VDVMVKRLHE YKRQLLKVLH VVSEYEGVIS
GRIPLEQLQP RTVVFGAKAA PGYAMAKRII HLINAVGSTV NADTRLDGRL QVLFPPNYNV
TLAESVIPAA DLSEQISLAG KEASGTGNMK FALNGALTIG TDDGANVEIR ELVGDENFFL
FGMAEPEVEA LSARGYRPSE FYQADAGLRR AIDLIASGSF SAGDRSVFEP IVSNLLYEDR
FMVLADYASY MAAQDRVDAA YRDGDRWIRS AILNVARCGF FSSDRSIHDY IDRIWHTPPM
I
//
