ID A8T3D9_9VIBR Unreviewed; 817 AA.
AC A8T3D9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 13-SEP-2023, entry version 54.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=malQ {ECO:0000313|EMBL:EDP59695.1};
GN ORFNames=AND4_11074 {ECO:0000313|EMBL:EDP59695.1};
OS Vibrio sp. AND4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP59695.1, ECO:0000313|Proteomes:UP000005159};
RN [1] {ECO:0000313|EMBL:EDP59695.1, ECO:0000313|Proteomes:UP000005159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AND4 {ECO:0000313|EMBL:EDP59695.1,
RC ECO:0000313|Proteomes:UP000005159};
RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA Milton D.L., Gonzalez J.M., Pinhassi J.;
RT "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT starvation.";
RL PLoS Biol. 8:E1000358-E1000358(2010).
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:EDP59695.1}.
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DR EMBL; ABGR01000003; EDP59695.1; -; Genomic_DNA.
DR RefSeq; WP_009842089.1; NZ_ABGR01000003.1.
DR AlphaFoldDB; A8T3D9; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000005159; 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: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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 664
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 817 AA; 92357 MW; 165DEF7D503E282F CRC64;
MKPTQQQKFD KQSFQTSVKK HLSTTYAHTT ENADSRAWYL AMGRALAEFT TCDLLDTEAD
ARIQEAKSVN YLSLEFLVGR LTGNNLISMG LYEQITEAMA ELGHNLTDLL EEERDPSLGN
GGLGRLAACF MDSCAAQEFP TVGYGLHYEY GLFKQSFKDG RQQEAPDAWR GVEGYPWELA
RPELAQEIGF YGHVEVVNEN GKEARKWVPG MSVKAMPWDL PIVGYESSTV YPLRLWECQA
IAPFSLASFN NGDYFEAQHA LIDAGNITKV LYPNDNHEKG KTLRLMQQYF HSAASVRDIL
RRHEAAGYSL EDLPKQETIQ LNDTHPTIAI PELMRILIDE RGLCWEAAWQ ISSQTFAYTN
HTLLPEALET WPESLVQRLL PRHMEIIFEI NHRFLQEVRS MWPGDGEKQA KLSIIQEGFN
RMVRMANLCV IGSYAVNGVA ALHSELVKKD LFPEFHEMYP TRLHNVTNGI TPRRWLKFCN
PGLSELITKK IGPEWPAKLE QLEGIAQYAT DAKFQKEFMA VKKENKERLA NWVIENMGIE
LDTNAIFDVQ IKRLHEYKRQ HLDLLHILSL YHRILNEPGF ECEPRVCFFA AKAAPGYHLA
KEIMFAVNKV AEKINNDPRI GNKLKVVFIP DYRVSMAEII IPAADVSQQI SLAGKEASGT
GNMKMALNGA LTIGTMDGAN VEIREEVGDE NIYIFGLDVE GVKAVRAAGY NPYDYYNADH
LLKASLDLLT GDEFTPGQPG LLRATFDSLL DGGDPYLCLA DFASYVKAHE EMGKQYKDQA
GWAKKAILNT ALVGKFTSDR SIRDYVNNIW KLKSVKR
//
