ID A0A1M5P2F2_9GAMM Unreviewed; 844 AA.
AC A0A1M5P2F2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Starch phosphorylase {ECO:0000313|EMBL:SHG95569.1};
GN ORFNames=SAMN04488068_1971 {ECO:0000313|EMBL:SHG95569.1};
OS Hydrocarboniphaga daqingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=490188 {ECO:0000313|EMBL:SHG95569.1, ECO:0000313|Proteomes:UP000199758};
RN [1] {ECO:0000313|EMBL:SHG95569.1, ECO:0000313|Proteomes:UP000199758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7049 {ECO:0000313|EMBL:SHG95569.1,
RC ECO:0000313|Proteomes:UP000199758};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; FQWZ01000004; SHG95569.1; -; Genomic_DNA.
DR RefSeq; WP_072896989.1; NZ_FQWZ01000004.1.
DR AlphaFoldDB; A0A1M5P2F2; -.
DR STRING; 490188.SAMN04488068_1971; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000199758; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199758}.
FT DOMAIN 14..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 608
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 844 AA; 94862 MW; 7EE91D7E1BAFA309 CRC64;
MPGTLFRLEL RPQIPPALSR LSDLASNLMY SWDRDIRGVF WRLDKDLWRA CGNNPKLFLR
RVSQAVLEAA ADDDDFLQDY HGALAAYDSY LAADAKPAVL AHLQPGQDLI AYFCAEFGLH
ESLPIYSGGL GILAGDHCKA ASDLGLPFVA VGLLYREGYF IQTIDGVGRQ VATPQTANFD
ELPIRLARDA TGNELRVAVP IADRIVQLRI WQADIGHIPL YLLDSDLPDN SEADRSITFQ
LYGGNTDTRI QQEIVLGVGG VRALRALGVA PSAWHINEGH AAFLILERVR EQVARGLDFD
SALENVAAGT VFTTHTPVPA GHDIFHHAQV QWFFQQLLPH YGADEARVLA LGADGHGETR
FNMTALALRG SRHHNGVSKI HGGVASTMER SLWPQITPAE NPIGSVTNGV HLHTFIARAW
TQLFHDSLRG WRNQLLDIDY WQRIDEIPDH RFRAVRRQLK RDLLIDIVER IERQHRRNEL
PEALIAQATQ HLRTHDTRTL VLGFARRFAT YKRATLILRD PARLSRLLND AQRPAILIFA
GKAHPKDQPG QDLIRQLHEM SLRPEFIGRL FMVEGYDMLL ARNLVQGCDV WLNNPEYPME
ASGTSGEKAG INGVVNVSVM DGWWAEGYQP EPQQNGFAIV PVLDPNIRDA EEARQLLDLL
EREVVPRYYG ADGDGYSAEW LRLSRNSMKS LIPRFNSSRQ VMDYVRGYYA PASAAARRLD
ADDAAQAREL AAWKQRVRQA WPGVSMRLAQ TPSSVVAAGE RLRLLVDVEL NGLDARDLVV
ECRVGRLDAH NQFVVQQVVT LAVDDGRWRA DVEPLCGLQH YQIRAYPHHR AQAHRFEMGL
MIWL
//
