ID U4KHJ7_9VIBR Unreviewed; 828 AA.
AC U4KHJ7;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:CCO61304.1};
GN ORFNames=VIBNI_B1561 {ECO:0000313|EMBL:CCO61304.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO61304.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO61304.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203527; CCO61304.1; -; Genomic_DNA.
DR AlphaFoldDB; U4KHJ7; -.
DR STRING; 28173.VIBNI_B1561; -.
DR KEGG; vni:VIBNI_B1561; -.
DR PATRIC; fig|1260221.3.peg.5155; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000016895; Chromosome 2.
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:UP000016895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 674
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 828 AA; 94637 MW; B980EAA4A29D5C79 CRC64;
MENQQREFQM KPTEHVNFNK EEFKNAVKKH LAATYATTVE NASERAWYLA TGRALAELTT
FDLLETENDP KIKNARSVNY LSLEFLIGRL TGNNLISLGL YDVVDEAVKE LGQNLTDILE
NERDPALGNG GLGRLAACFM DSCAAQQFPT VGYGLHYEYG LFRQSFEDCH QKEAPDAWAG
VEGYPWEVAR PELAQQAGFY GHVDVYVNDD GVEKRRWKPG MYVQGMPWDM PIVGYQSRTV
YPLRLWECRA IAPFSLESFN NGDYFEAQHA LIDAGNVTKV LYPNDNHEKG KTLRLMQQYF
HVRCSMADIL HRHQANGHSL EDLPKYETIQ LNDTHPTVAI PELMRVLVDE NDFEWDDAWA
ICTKTFAYTN HTLLPEALET WSEALLQRLL PRHMEIIYHI NHLFLHDVKE KWPGDVDKMR
KLSIIEEGTH RMVRMANLCV VGSYAVNGVA ALHSALVKKD LFPEFNEMFP GRLQNVTNGV
TPRRWLKFCN PELSELITSK IGEDWIVDLD ELRKIEKFAD DETFQQDFMR VKQANKQRLA
DWVKENMGIE LDTNAIFDVQ IKRLHEYKRQ HLNLLHILSL YHRLLNDPKF DMAPRVVFFA
AKAAPGYHLA KEIIFAINKV AEKINNDNRV KHKLKVVFMP DYRVSMAEII IPAADVSEQI
STAGKEASGT GNMKLALNGA LTIGTMDGAN VEIREEVGDD NIYIFGLEVE EVQALREKGY
NPYDYYHADH LLKASLDLLV GDEFTPGQPG RLAATYESLL DGGDPYLVLA DFASYIKAHE
DMDVQYRDQK GWARKAILNT ALVGKFSSDR SIRDYVNNIW KLEAVKRS
//
