ID I0HFU0_ACTM4 Unreviewed; 812 AA.
AC I0HFU0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=AMIS_66570 {ECO:0000313|EMBL:BAL91877.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL91877.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL91877.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) 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}.
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DR EMBL; AP012319; BAL91877.1; -; Genomic_DNA.
DR RefSeq; WP_014446762.1; NC_017093.1.
DR AlphaFoldDB; I0HFU0; -.
DR STRING; 512565.AMIS_66570; -.
DR KEGG; ams:AMIS_66570; -.
DR PATRIC; fig|512565.3.peg.6662; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000007882; 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:UP000007882};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 660
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 812 AA; 91083 MW; AE126AE935329EA2 CRC64;
MDLRQGIGLR KLGRTVDEFQ QDLLSNLYFR RGTTVESASM RDAYETLSLT VRDHLAERRA
RTAAAHYASN PRWVYYLSAE YLLGAQLEQN LLYSGTGEIA AQAVKSFGLT LEEIEELDVE
PGLGNGGLGR LAACLVDAMA TRDIPAVGYG IRYDFGIFKQ SLAAGGQAEG PDDWAFQGNP
WEFPAPDDRQ TVGFYGHTEP VPGSSTRKVW VPGEIVLGEP SHMLVPGYGT DTVNIVRLWR
ARGSEASFDL SRFSAGQYAE AVQEAVRAEN ISKVLYPDDS TELGRELRLK QQYFLVSCSL
RDIIRRFRLR NEGWDDFPEK TVIQLNDTHP TIAIPELMRL LVDEYELDWD RAWSITRRTF
AYTCHTLLPE ALETWPVHVF ERLLPRHLEI IYLINMLFLR EVEERFPGDV ARVSRMSIIG
EHPERRVRMA NLAVVGTEAV NGVAELHSKL LRETVLNDFA DLWPAKFQNV TNGISPRRFV
KLANPRLSDL ITEGLGDDGW LMDLERLAEL GSLAGDASFL ERWRAIKRAN KVDLAVGDPD
SLTDVMIKRF HEYKRQQLKL LHIITLYHRI RANPGGDWVP RTVLFAGKAA PAYHAAKNII
RLINAVGATI AADPIVSPYL KVVFAENYNV SLAERIVPAA DLSEQISLAG KEASGTGNMK
LALNGALTIG TLDGANIEIR ARVGEENFFL FGLDAFQAAE LQIAGYRPWE HYERDPELRE
ALDAINAGLF GGVGHDVADS LLGRDEYLTL ADYRAYVDCQ DEVERAWRDQ DRWTRMSVMN
TANSGFFSAD RTVADYAARI WRVAPVPVAK DH
//
