UniProt: A0A376BJV6

Database: UniProt
Entry: A0A376BJV6_9NEIS

LinkDB:  A0A376BJV6_9NEIS 
Original site:  A0A376BJV6_9NEIS

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
All databases (13)   

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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
//

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