ID A0A0P0G8K6_9BACT Unreviewed; 824 AA.
AC A0A0P0G8K6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 {ECO:0000313|EMBL:ALJ56885.1};
GN ORFNames=AMD24_00723 {ECO:0000313|EMBL:ALJ56885.1};
OS Candidatus Xiphinematobacter sp. Idaho Grape.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Xiphinematobacter.
OX NCBI_TaxID=1704307 {ECO:0000313|EMBL:ALJ56885.1, ECO:0000313|Proteomes:UP000062177};
RN [1] {ECO:0000313|EMBL:ALJ56885.1, ECO:0000313|Proteomes:UP000062177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Idaho Grape {ECO:0000313|EMBL:ALJ56885.1,
RC ECO:0000313|Proteomes:UP000062177};
RX PubMed=26362082; DOI=10.1093/gbe/evv176;
RA Brown A.M., Howe D.K., Wasala S.K., Peetz A.B., Zasada I.A., Denver D.R.;
RT "Comparative Genomics of a Plant-Parasitic Nematode Endosymbiont Suggest a
RT Role in Nutritional Symbiosis.";
RL Genome Biol. Evol. 7:2727-2746(2015).
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; CP012665; ALJ56885.1; -; Genomic_DNA.
DR RefSeq; WP_062100696.1; NZ_CP012665.1.
DR AlphaFoldDB; A0A0P0G8K6; -.
DR STRING; 1704307.AMD24_00723; -.
DR KEGG; xii:AMD24_00723; -.
DR PATRIC; fig|1704307.3.peg.806; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000062177; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000062177};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 661
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 824 AA; 94109 MW; DD1C898547821E4A CRC64;
MTDTSSVPEL KKLIYNQLRL GLVRDPETAT LRDWWISTSK AARTIIIERL IATQREHYRK
NVKRVYYFSL EFLMGRLFSN SLHNVGIFSQ IQQAIGEMGL SLDSLREEEY DMALGNGGLG
RLAACFMDSL ATMDFPAIGY GIYYQYGLFK QEFHNGYQAE LPDDWMHLFG SPWEIKRPEY
ATEVQLYGRV ENVFDEYGNC VQKWVNTKKV LGIPHDIPVP GFGTKTVNYL RLWASHADKS
FDFEAFNRGE YDKAILEKNC SEILTKVLYP NDKTERGREL RFIQQYFFVS CSLQDILRRF
LKNNDNWEHL PEKAAIQLND THPAIAIVEL MRIFLDLYAM PWEQAWSIVT RVFAYTNHTL
LPEGLEKWSV ATFSAILPRH LQVIYEINSK LLEQVEKKWP HNTSKRCALS LIEEGREKMV
RMAHLCVVGS HSVNGVAALH TQLLKQHLFS EFHALYPSKI NNKTNGITPR RWLLACNPRL
SVLITSKIGD SWIRNLSRLR ALEDYIEDPE FQQDFMAAKL ANKTFLASLI QQECGITVDP
SALFDVQIKR LHEYKRQHLN LLHILALYRR LLQNPNLDIV SRVFVFAAKA TPGYDMAKCI
IKAINSVGSV INRDSRISGK LKVAFLPNYR VSLAQRIVPA ADLSEQISTA GKEASGTGNM
KMALNGALTI GTLDGANVEI CEEVGEENIF LFGLKINEVA ALLRKGYCPE EFYHADEELR
AVIDWLGSGY FTPCDPPGTL NPLLESLIHQ DPFLVLADFR SYSDCQQRVD ATFRDKSLWA
RMAIFNTARV GKFSSDRAVG EYAREIWQLD PVPVLGAELN RCIP
//
