ID   D2RP29_ACIFV            Unreviewed;       805 AA.
AC   D2RP29;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   10-JUN-2026, entry version 79.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   OrderedLocusNames=Acfer_0402 {ECO:0000313|EMBL:ADB46805.1};
OS   Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS   106432 / VR4).
OC   Bacteria; Bacillati; Bacillota; Negativicutes; Acidaminococcales;
OC   Acidaminococcaceae; Acidaminococcus.
OX   NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB46805.1, ECO:0000313|Proteomes:UP000001902};
RN   [1] {ECO:0000313|EMBL:ADB46805.1, ECO:0000313|Proteomes:UP000001902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4
RC   {ECO:0000313|Proteomes:UP000001902};
RX   PubMed=21304687; DOI=10.4056/sigs.1002553;
RA   Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Acidaminococcus fermentans type strain
RT   (VR4).";
RL   Stand. Genomic Sci. 3:1-14(2010).
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; CP001859; ADB46805.1; -; Genomic_DNA.
DR   RefSeq; WP_012937795.1; NZ_CP085936.1.
DR   AlphaFoldDB; D2RP29; -.
DR   STRING; 591001.Acfer_0402; -.
DR   KEGG; afn:Acfer_0402; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_9; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000001902; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000003; Alpha-1,4 glucan phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000807; Alpha-glucan phosphorylase 2, cytosolic; 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, LIVER FORM; 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   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
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:UP000001902};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         658
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   805 AA;  92841 MW;  A47861DEB2C3089C CRC64;
     MTKNWKSPKQ FVCLFTQKAK ILFNEEPAAL TPKKVYLVLA NLVKDLIYDD WLATEQRYDA
     RQTKQVYYFS IEFLLGRLLD ANLMNCGMEN MAREGLKELG FDLDAIMPLE ADPGLGNGGL
     GRLAACFIDS LAALQLPGHG CSIRYQYGLF EQHIVDGQQV ELPDTWLQDG FPWETKRSDK
     AVHVRYGGSA YMRPDGKGGL ECVHEGYSSV LAIPYDVPVP GYRNHTVNTL RLWQAEYTPD
     GLFGQGQGGD FRKVLQYRDT TQQISRFLYP DDSTEEGRKL RLMQEYFFVS AGLQSIVRHY
     RGQHRDLREF DRYVALHIND THPALLIPEL MRILMDEEGM GWEEAWRITV ASTSYTNHTI
     MPEALERWSI PLFQSLLPRV YLIVEELNRR WLAAYRRKFP GREDKAEQVA ILWGGQVRMA
     NLAVVGSHSV NGVAELHTKI LEESTLHPFY EVYPERFNNK TNGVTHRRWL LESNPPLAAL
     ISDTIGTDWI RHPKKLKELL PYRDDPSFQE KLAQVKQDRK DALVRWIQET RGVAVDPHSL
     FDIQIKRFHM YKRQLLNILH VYSLYLRLLD DPDAVPLPQT FLFGGKAAAS YGEAKVVIKL
     IHTVARLIDQ EPRVREKLKV LFLENYNVSL GQRLFPAADV SEQISTASKE ASGTGNMKFM
     MNGAITLGTL DGANVEIHRL VGDENCVIFG LRAEEVQKYY REGGYSSWDL YRQDEEIRRV
     LDVFQKNPLF SQLYEDLLRR NDEYFVLKDF AAYREAHQEI LRRYQDRPGW LRASAVNIAQ
     SGHFSSDRTV SQYARDIWKV KPIRV
//