ID B2HRY4_MYCMM Unreviewed; 838 AA.
AC B2HRY4;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=MMAR_2568 {ECO:0000313|EMBL:ACC41014.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41014.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC41014.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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; CP000854; ACC41014.1; -; Genomic_DNA.
DR AlphaFoldDB; B2HRY4; -.
DR STRING; 216594.MMAR_2568; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; mmi:MMAR_2568; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_11; -.
DR Proteomes; UP000001190; Chromosome.
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:UP000001190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 838 AA; 94247 MW; 60EA501B7351FC20 CRC64;
MSDVILPAAQ AATAATNVGD VRTGMSSDAL RQAIEDHLRY SLGRPAALLE PKHYYRALAL
AVRDRMQQRW IETTQTYLDL SRKVACYLSA EFLLGPHLGN NLLNLQIEEE ARAALTALGQ
DFDEVLACEE EPGLGNGGLG RLAACYLDSL ATLQRPAVGY GIRYEFGIFD QEIRDGWQVE
KTDNWLADGN PWEIVKPELN YRVGWGGRTE SYIDERDRYR VRWIPQRAVK GVYYGTPIQG
YGVNTCNTLT LWSARAIQSL ALDAFNAGDY YRAVDDQVVS ETVTKVLYPN DEPEVGKQLR
LAQQYFFVSC SLQDILHLLE DFAGLPVQEL PNRVAIQLND THPSIAVADL MRLLVDERDL
DWEEAWRITV ASLAYTNHTL LPEALETWPL SMFERFLPRH LEIIYEINRR FLDEVRARFP
GDENRVRRMS LIGEDGDRSI RMAHLAIVGS HAVNGVAALH SELLKTTVLK DFYEMWPQRF
SNKTNGVTPR RFVALANPGL RKLLDETLGP GWLRNLDRLS ELAPLAGDPA FQQRWRAVKR
TNKARLSDYV RSCTGIELDP DWLFDIQVKR IHEYKRQHLN VLHIITAYHR LKLNPNLEIA
PRAYIFGGKA APGYMMAKLI IKLINSVAEI VNSDPDVNDR MKVAFIPNFN VQSGQMIYPA
ADLSEQISTA GKEASGTGNM KFMMNGALTI GTLDGANVEI REQVGAQNFF LFGLTVQDVQ
RVLAAGYRPR DYIRENAELS AALGLIGSGA FSGGDPEVFA PLIANLSERD PFLVNADYAD
YLRAQQEVSN TWQDTESWTR KSILNSAYSG KFSSDRAIAE YCDDIWNIAA VTIGSRPD
//
