ID A0A376BJV6_9NEIS Unreviewed; 827 AA.
AC A0A376BJV6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:SSY70001.1};
GN ORFNames=NCTC10283_00064 {ECO:0000313|EMBL:SSY70001.1};
OS Alysiella crassa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Alysiella.
OX NCBI_TaxID=153491 {ECO:0000313|EMBL:SSY70001.1, ECO:0000313|Proteomes:UP000254209};
RN [1] {ECO:0000313|EMBL:SSY70001.1, ECO:0000313|Proteomes:UP000254209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10283 {ECO:0000313|EMBL:SSY70001.1,
RC ECO:0000313|Proteomes:UP000254209};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
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DR EMBL; UFSO01000002; SSY70001.1; -; Genomic_DNA.
DR RefSeq; WP_034294753.1; NZ_UFSO01000002.1.
DR AlphaFoldDB; A0A376BJV6; -.
DR STRING; 1120980.GCA_000745955_02135; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000254209; 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:UP000254209};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 669
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 827 AA; 94532 MW; B46C2A0AD2141D9C CRC64;
MSNNALQFQE YEYAMPQPNA ERIRQSIVYK LIFILGIDPK DATPENWLNA AMFAARDLMT
ESFLHTRRAH ESQRKRMVYY LSMEFLMGRA FTNALINQNL YEPFAQAFKE LGLDLGEISE
HEADPGLGNG GLGRLAACFL DSLATLRIPA MGYGIRYQYG MFKQEIVDGQ QVEKPDLWLD
NDMAWQFSRP NKRFLVHFGG HCVHFDGKVT WQPAEQISAI AYDEIVPGFG AQVANPLRLW
TAHTGDLFDL SKFNRGDYFA AMEQQQKNEN IANVLYPNDD TNEGKVLRLK QEYFLVSASV
QDIIDRHLCR FPNIKTLADE VAIHLNDTHP VLAIPELMRV LMDEHHLPFD EAWAMCQKIF
SYTNHTLMSE ALEKWSVNLM LNLLPRHLDI IYKINSVFLE QVKASGYDDD FVRRVSIIVD
EHDGQQVRMA WLAVIASHKI NGVAKLHSDL MVSSLFADFA KLFPERFTNV TNGVTPRRWI
AVANPPLAAL LDKYLETSDW RIHLDKLVKL NEFSGSLQVQ QEFADVKRAA KVRLADYVER
ELGIKISPDA LFDVQIKRIH AYKRQSMNIL HIVHRYFQIL DNPNADWQAR VFILAGKAAS
AYHEAKHTIR LINDVAKVIN NDSRVRDLIK VVFIPNYSVS LAQLIIPAAD LSEQISLAGK
EASGTSNMKF ALNGALTIGT LDGANVEIHE RVGDEHSFIF GNTVEQVEAL YARGYNPYEF
VDNDPDLRRV FHAIANGHFS PEETSRYSAL MHNGDHFQRY ADFRAYVDTQ LKVDAHYRDQ
AAWRKSAIIN IANMGYFSSD RSIEDYCRDI WYIKPLTEQE LPNNGRG
//