ID A0A0B7NLZ8_9FUNG Unreviewed; 709 AA.
AC A0A0B7NLZ8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 40.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN Name=PARPA_13967.1 scaffold 47516 {ECO:0000313|EMBL:CEP19651.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP19651.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP19651.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP19651.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000256|ARBA:ARBA00000370};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
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DR EMBL; LN734065; CEP19651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NLZ8; -.
DR STRING; 35722.A0A0B7NLZ8; -.
DR OrthoDB; 313745at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd16011; iPGM_like; 1.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR045216; CK2_alpha.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; TIGR00306; apgM; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 44..313
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 709 AA; 79974 MW; 1BC8BCB2760D6BA6 CRC64;
MSSSANTSNC KSIARCYADV NANMPTSYWD YDNLQVEWGN QENYEIIRKV GRGKYSEVFQ
GIDIVNNEKC IIKALKPVKK KKIRREIKIL QNLAGGTNML DFWALLGTLF QKHLPSSPMY
DIQYYMYELL KALDYCHSKG IMHRDVKPHN VMIDHEKKEL RLIDWGLAEF YHAGTEYNVR
VASRYFKGPE LLVDFQEYDY SLDLWSYGCM FASMIFRKEP FFHGHDNYDQ LVKIARVLGT
DELFRYTEKY SITLAPEYNN ILGRHMRKPW NKFITSENQR FVTDDSIDFL DKLLRYDHQE
RLTAKEAMAH HYFDGLGDVN IPNLASKTPL QYAHTPWLDK LCDPVEPGLA CGSDTAHMSI
LGYDPRRYYE GRGAFESMGA GLDMIPSDIA FKSNFAYLDK ESGIVVKRKA DRNFQDIGPI
LCNAIDDVKL PSFPDHSVSV KYAIEHRCGV RVRGPGLTSS ITGTDPLVDN KPLIHCEPTL
DNEASLTNEL SDAFYNILID HPINKERIKA GKNPANCVLL RGCGSCIDVP SIEKLHGLKS
FLIAPTCIIA GIGMTLGMDL IDVPGATGDY NTDFAAKAKA CLDNIQSGDY DFGFCHVKAV
DDAGHDHDFL KKVHYIEKTD RMIGTVVSTL EQSAGIKYTI IVTGDHTTPA LYGDHSCEPV
PFVISSIQND MQREGDSVRT FNEIAAAQGA LGRFCGDQIM PLAKSFMQL
//
