ID A0A1M7YMS4_9FIRM Unreviewed; 1255 AA.
AC A0A1M7YMS4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SAMN02745217_04345 {ECO:0000313|EMBL:SHO53882.1};
OS Anaerocolumna xylanovorans DSM 12503.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1121345 {ECO:0000313|EMBL:SHO53882.1, ECO:0000313|Proteomes:UP000184612};
RN [1] {ECO:0000313|EMBL:SHO53882.1, ECO:0000313|Proteomes:UP000184612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12503 {ECO:0000313|EMBL:SHO53882.1,
RC ECO:0000313|Proteomes:UP000184612};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};
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 disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; FRFD01000015; SHO53882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7YMS4; -.
DR STRING; 1121345.SAMN02745217_04345; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000184612; Unassembled WGS sequence.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR00217; malQ; 1.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000184612};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
SQ SEQUENCE 1255 AA; 145889 MW; 06A7D1388EC79A08 CRC64;
MREAGVLMPV ASVSADYGVG DFGKQTYEFI DILKKSNISI WQILPLNPLG YGESPYQPYS
SMAGDEIYID LVRLYEEGLL ADVPPAFRKT STKIKYQEVR KYKEKYLKMA FKAFLPDKEY
EEFIEQEWVY LYGVFLTLKK KNELKCWNEW KTEHKNWIQD RRFDETVYEK DIRYEMFVQY
EFYRQWMALK SYANHSGIQI MGDVPFYVGI DSLDVWTNQE DFLLDKDGHP VFIAGVPPDY
FSRTGQRWGN PIYNWERMEE NNFHFWLERF GYTAKLFDII RIDHFRAFDT YWKIPASCDT
AIEGEWLEAP GYELFDLLLK TYPDIHIVAE DLGEMRPQVY ELRDHYSLKG MKIIQFSFDP
LEGNNGFPDR ENMMVYTGTH DNETILGWFE NQSGQVQNET ELELYAYGYV SGSISHKFIR
YTLDNLAEIA IIPVQDILEM GNEGRINTPG TLGSPNWEWK LSSLEELHAQ TEFLAAAVTE
SGRFGEIRKV TEKIKDSARL LTKLLEQQFG KTIGACTREE LLLGLLGMVK RLAADRTERD
EKRKLYYISA EFLIGKLLSN NLINLGIYED MRELLAASGQ DLTEIEEAEP EPSLGNGGLG
RLAACFLDSI ATLGLAGDGI GLNYHLGLFK QHFKDFLQKE EKNPWMEKAC WLTKKKNSYE
VEFGSFKVKS ILYNIDVIGY QNRNNKLHLF DSELVDEGLV EEGIEFDKKD IKKNLTLFLY
PDDSDEAGRQ LRIYQQYFMV SCGAQLILEE SVRRGSDLHD LYEYAVIQIN DTHPSLVIPE
LIRLLIKRGI ALDEAISIVT KTCAYTNHTI LAEALEKWPL DYLKKVVPQL VPIIEILDNR
VRRKYGKEEV AIIDSRERVH MASMDIHYGF SVNGVAALHT DILKTTELNH FYKLYPEKFN
NKTNGITFRR WLLHCNRELA FFIESLIGDG FHKDSMELNK LIHFRKEERV LSRLLNIKYQ
NKRKLKSWLE KDQGITIDEN SIFDIQIKRL HEYKRQQMNA LYVIYKYQEI KDGKLPEIPI
TVIFGAKAAP AYIIAKDIIH LILCLQELIN NDPQVSPYLK VVMVEDYNVT KAEVLIPACD
ISEQISLASK EASGTGNMKF MLNGAVTLGT LDGANVEISD LVGGENIYLF GETSDQVIRH
YQKADYISKR YYQKDDDIKK ALDFIISERM LAIGQKENLQ RLYKEILNKD WFMSLLDFKD
YIRAREEAYT DYKDRLGWAE KMLVNISKAG YFSSDRTIRE YNEQIWKLDG DIKRK
//
