ID A0A083ZVD4_9GAMM Unreviewed; 812 AA.
AC A0A083ZVD4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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_4 {ECO:0000313|EMBL:KEY57013.1};
GN ORFNames=SRDD_40320 {ECO:0000313|EMBL:KEY57013.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY57013.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY57013.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY57013.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
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:KEY57013.1}.
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DR EMBL; AYKS02000108; KEY57013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A083ZVD4; -.
DR STRING; 1410619.SRDD_40320; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000017810; 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:UP000017810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 665
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 812 AA; 91071 MW; 4A9D9867DEC122B3 CRC64;
MNTKQTRVEL PGVDEIKNNI ISKLRYSLCL ELQDATDADI FNALALTIRD YQLDGFFETK
GYQEAAKSKR LYYLSMEFLL GQSLRNNLMN VGLLSAASQA IGELGFDFDA IVGQEPDAAL
GNGGLGRLAA CFIDSMATLD IAASGHGIKY EYGLFKQSIQ NGKQVEQPDD WHATHSPWLI
DHHSQLMLIP VGGHIEVTED IDGNYNPMWM DWKVIVGVPH DYFVTGYGGK TVNKLRLYSA
SASDSFDVHI FNRGDYLRAV SQKIASENIS KILYPADEIQ SGKELRLTQE YFLVACTLRD
IFQEFATRSE DITTLPDAVA IQLNDTHPAL AIVEMMRILV DEHRLDWDIA WGITQKTCAF
TNHTLMPEAL ETWPVTLFEK LLPRHLQIIY EINHRHLSEV AEKWPDRPEL LASLSLFEEG
GEKKVRMANL AIVGSHKVNG VAKLHSELIK QELVPNFYFI SPEKFTNQTN GVTPRRWIQQ
ANPRLATFLT RELGPGWVTD LDKLQGLKKL ANDSGVLEEL QTIKLHNKRA LCQLVATRQG
VKLDPQALFD SQVKRIHEYK RQLLNILHVI HLYLGIVESG NTLQPKVHLF SGKAAPGYAM
AKLIIQLINE VARTINNDPR AKGQLNVLFL EDYKVSLAEH IIPATDLSEQ ISTAGTEASG
TSNMKFAMNG ALTIGTMDGA NIEIRDAVGA DNFYLFGANA AEINAHRFAG SHNHVYSNNP
VTREAVDALV SGRFNLDKSL FLPIYRMLTE GDHYCHLLDF DSYCVAQEQV LHDFAHQQQW
HRRALLNIAG MGLFSSDRTI KGYATEIWGI PC
//
