ID A0A2H9U183_9GAMM Unreviewed; 824 AA.
AC A0A2H9U183;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CUC53_16245 {ECO:0000313|EMBL:PJG57760.1};
OS Aeromonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1006623 {ECO:0000313|EMBL:PJG57760.1, ECO:0000313|Proteomes:UP000235861};
RN [1] {ECO:0000313|EMBL:PJG57760.1, ECO:0000313|Proteomes:UP000235861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDC 2508 {ECO:0000313|EMBL:PJG57760.1,
RC ECO:0000313|Proteomes:UP000235861};
RA Colston S.M., Navarro A., Martinez-Murcia A.J., Graf J.;
RT "Draft genome sequence of environmental isolate Aeromonas cavernicola sp.
RT nov. MDC 2508.";
RL Submitted (NOV-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PJG57760.1}.
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DR EMBL; PGGC01000172; PJG57760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9U183; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000235861; Unassembled WGS sequence.
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:SF25; MALTODEXTRIN 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 670
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 824 AA; 93240 MW; 5FA6A86BF73BCEB3 CRC64;
MATKKHTGQD LQLDKDQLKA SIVRHLRSTL GTSEQKASPD AWWKATAAAV NEQVYERLTR
TQQTHFKKDT RAIHYLSAEF LMGRLTSNNL HNLSLYKVCE EALADLGLDL TDLCEQEPDM
ALGNGGLGRL AACFIDSLAT LNYPAVGYGI HYEHGLFRQE IQDGRQIERP DSWREYGNPW
EICRPESVQE IPLYGYVETV FGDNGGLKKV WHAGRKIKGV PWDIPVVGFG GHTVNILRLW
ESRASEFFDW DVFNAGGYVN SQAEKAQAET ISKVLYPNDE TDAGKELRLI QQYFFCACSI
KDIMRRYKRA HGNDFSQFAA QIAIQLNDTH PTVAIPELMR VLVDEEGLNW DSAWSICYHV
FSYTNHTLLP EALEKWSVHL FEKVLPRHLE VIYEINARFL DELVEPKWPG NDAIKAKLSI
IEEGAVRKVR MGNLCVIGSS KVNGVAEIHS KLVKEDLFPE FAQLWPEKMC NVTNGVTPRR
WLLACNPELS ALYDDAVGNT WPLALDKLRE VVKSADDPQF QQKFMAIKRR NKEKLVKVIK
AETGIEVSAE AIFDVQIKRL HEYKRQQLNL IHIMALYRRL LTNPDYQMHP RVFIFGSKAA
PGYKLAKDII YAINKLADRV NNDTRIQGKL KVVFMPNYRV SLAEKLIPAA DVSEQISTAG
YEASGTGNMK LALNGAVTIG TLDGANIEIA EEAGAENCAI FGLNVDEVKT LKARGYNPYD
FYYGNSELKA VLDWFDTDYF TPGRPGELAA IKHSLLEGGD PYLTLADFHS YSEAHKLIDT
WYRDPALWAR KAIINSATMG KFNSDRSIQD YVDRIWKLTN CNVG
//
