ID A0A080M9V2_9PROT Unreviewed; 859 AA.
AC A0A080M9V2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=malP_1 {ECO:0000313|EMBL:KFB77235.1};
GN ORFNames=AW06_001649 {ECO:0000313|EMBL:KFB77235.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77235.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB77235.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:KFB77235.1}.
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DR EMBL; JDST02000031; KFB77235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M9V2; -.
DR STRING; 1453999.AW06_001649; -.
DR Proteomes; UP000021315; 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: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:UP000021315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 687
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 859 AA; 98318 MW; 043B925ECB552D2B CRC64;
MNVEMEKENA PPVEAVGDLL VGREERRTGL SVDALRRAIL DKLVYVQARF PQVATRRDCF
MALAQAVRDR LLQRWVQTAR TYRDRGSRTV CYMSAEFLIG PQLGNNLINL GIFDKARQAT
QEFGLDLEML LDQEEEPGLG NGGLGRLAAC YLDSLATLEI PAIGYGILYE FGIFTQAIRD
GQQVELTDKW LRAGSPWLIH RPSIAFDIKL GGHTEFQFEA NGERRLRVQW IPAKVVRGTA
WDMPVLGYGV NTPNRLRLWS AEAPESFDFA AFNAGNYYQA VDAQIRSETI TKVLYPNDET
EAGQELRLEQ QYFFVACSLK DMIRLQLQRE KNLDHFDEKF VIQLNDTHPS IAVAELMRLL
VDEYMMEWDP AWAITRKTFA YTNHTLLPEA LEKWRLALFK RVLPRHFEII CEINLRFLDE
VRIRYPGDDA RLRRMSLIDE DGAHYVRMAN LAVVGSFAVN GVARLHSELL KSDVLKDFYE
MWPEKFNNKT NGVTPRRFVV LANPTMSGLI EETIGPGWVT DMKRLRELEP YADDPAFRES
WRRIKTGNKS RLVGEIKRFV HVDVDPASMF DVQVKRLHEY KRQHLNILHV VSLYKRLKDN
PDLVIAPRTV IFGGKAAPGY FMAKLIIRLI NAVADVIGRD PAMHGKLQVV FFPNYNVKHA
QSIFPAADLS EQISLAGKEA SGTGNMKFQM NGALTIGTLD GANVEIREEV GDDNFFLFGM
STPEVMELRR TGYRPRTYYD ANPHLREVID LIASGFFTKG DREIFRPLID HLLNHDEYMV
LADFQSYIDC QARVSEAYLD VDRWTRMSIL NVARSGFFSS DRAIREYCDE IWNVKPVRIE
LSHLSGEDMQ FTRAIAGAD
//
