ID A4T1K1_MYCGI Unreviewed; 827 AA.
AC A4T1K1;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Mflv_5144 {ECO:0000313|EMBL:ABP47610.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP47610.1};
RN [1] {ECO:0000313|EMBL:ABP47610.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47610.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP47610.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47610.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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 -!- 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|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; CP000656; ABP47610.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T1K1; -.
DR STRING; 350054.Mflv_5144; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; mgi:Mflv_5144; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_11; -.
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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587,
KW ECO:0000313|EMBL:ABP47610.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Transferase {ECO:0000256|RuleBase:RU000587, ECO:0000313|EMBL:ABP47610.1}.
FT MOD_RES 672
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 827 AA; 93203 MW; 92FFD1396D3A4E97 CRC64;
MNGSAVGPTG QTRSGMSADA LRAAVRDHLV YSIARPAAVL TPEHYYRALS LAVRDRMQKR
WMATTQDWLD LSAKVTCYLS AEFLMGPQLG NNLLNLGIEK QAREALSDLG QDLDEVLACE
GEPGLGNGGL GRLAACYLDS LATLERPSIG YGIRYEFGIF RQEISDGWQV EKTDNWLVRG
NPWEIDKPDA SYVVNWGGHT EQYEDVTGRL RVRWVPQRVL QGVSYDTPVQ GYGVNTCNTL
TLWSARAVES FALEAFNTGD FYKAVDEEVV SETVSKVLYP NDEPEAGKRL RLLQQYFFVT
CSLQDILSIH LKRAHLPLHR LPDKWAIQLN DTHPSIAVAE LMRLLIDEHH LAWDDAWDLT
VRTFGYTNHT LLPEALETWP LRIFGEALPR HLELIYEIND RFLDEVRARF PGDEERVSRM
SLIGEDGGKS VRMAHLATVG SHAVNGVAAL HSELLKQSVL KDFYEMWPER FGNVTNGVTP
RRFLALSNPG LRALIDDTIG PGWLTDLERL HGLESFVDDP AFRLRWREVK RANKSRLAEY
VHSITGIELD PTWMFDVQVK RIHEYKRQHL MVLHIIALYQ RLKNNPGLTI PPRAFIFGGK
AAPGYFMAKR IIKLITAVGD TINADPEVNR CMKLVFLPNF NVKNAHLVYP AANLSEQIST
AGKEASGTGN MKFMINGAVT IGTLDGANVE IRQEAGAENF FLFGLTESQV EKVKADGYRP
LSHVENDAEL AGVLELIARG EFTHGDTEVL RPIVDNLVHH DPFLVLADYR SYVDCQDEVS
RAWLDRDAWS RMSIRNTARS GKFSSDRAIR EYCDEIWGVR PMSVDLE
//
