ID A0A161U443_9MICO Unreviewed; 843 AA.
AC A0A161U443;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:KZE90651.1};
GN ORFNames=AVP41_00170 {ECO:0000313|EMBL:KZE90651.1};
OS Microbacterium sp. TNHR37B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE90651.1, ECO:0000313|Proteomes:UP000076535};
RN [1] {ECO:0000313|EMBL:KZE90651.1, ECO:0000313|Proteomes:UP000076535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE90651.1,
RC ECO:0000313|Proteomes:UP000076535};
RA Adelskov J., Patel B.K.;
RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT Great Artesian Basin of Australia.";
RL Submitted (JAN-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}.
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:KZE90651.1}.
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DR EMBL; LQGV01000001; KZE90651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161U443; -.
DR STRING; 1775956.AVP41_00170; -.
DR PATRIC; fig|1775956.3.peg.175; -.
DR Proteomes; UP000076535; 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:UP000076535};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 692
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 843 AA; 94671 MW; 156DA6FE042E2FA5 CRC64;
MYLRKVPEND FAAAPASHPL HATHPLALAP VTGPASSVDG FVRQFLRNLN YERGVPLSAS
SVTDRYYAFA MTVRDYLMAR WLEDQRRQRE QQAKGVCYLS AEYLLGRQLD NNLLASGLTD
IATEAMAACG IDIDELRAQE VEPGLGNGGL GRLAACFIDS LATLSVPNIG YGIRYEYGIF
RQTFVDGQQV EQPDAWLAMD TPWEFPHPEA AQEISFGGHT ETYDDDGVIR SRWIPGWNVQ
ALPYNYMVPG YQNGRVNTLR LWSAKATDSF DLRVFNSGDY EEAVRAQTFA ENISKVLYPE
DSTPQGKELR LQQQYFFVAA SIADFLQHQL ADGFDLSGLP DRVIFQLNDT HPVIAVPELM
RVLVDEKKLE WEEAWRITQG CFAYTCHTLL PEALEVWPVD LLGRLLPRHL EIIYRINDEF
LAAVRERFGD DEMRIRNMSI IGEVPVRSVR MAYLATVAGA KVNGVAELHS QLLRDKVLPD
FNEFYPGKFT NVTNGVTPRR FVRLANPELS GLITEALGTG WITDLERLRE LESYAEDPEF
RARFREVKAA NKRRLSHVLH TRDGFDVSDG HMLDVMVKRL HEYKRQMLKL LHIVTAYEGI
VSGRVDVAEV QPRTFIFGAK AAPGYVMAKQ IIHLINAVGS VVNADPRVAD RLKVLFPPNY
NVTLAERVIP AADLSEQISL AGKEASGTGN MKFALNGALT IGTDDGANVE IRELVGDDNF
FLFGMSEPEV EALWARGYRP ADFYQADEGL RRAIDLIASG AFSGGDKSVF EPIVSNLLYD
DRFMVLADYS SYIQAQATVD AAYQDQDAWT RSAILNVARC GFFSSDRSMR DYIERIWHTP
PVL
//
