ID A0A095C8M4_CRYGR Unreviewed; 551 AA.
AC A0A095C8M4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00021932};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN ORFNames=CNBG_2828 {ECO:0000313|EMBL:KGB76990.1};
OS Cryptococcus gattii serotype B (strain R265) (Filobasidiella gattii)
OS (Cryptococcus bacillisporus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus gattii species complex.
OX NCBI_TaxID=294750 {ECO:0000313|EMBL:KGB76990.1, ECO:0000313|Proteomes:UP000029445};
RN [1] {ECO:0000313|EMBL:KGB76990.1, ECO:0000313|Proteomes:UP000029445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R265 {ECO:0000313|EMBL:KGB76990.1};
RX PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA Birren B.W., Galagan J.E., Cuomo C.A.;
RT "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT immunocompetent hosts.";
RL MBio 2:E342-E342(2011).
RN [2] {ECO:0000313|EMBL:KGB76990.1, ECO:0000313|Proteomes:UP000029445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R265 {ECO:0000313|EMBL:KGB76990.1};
RX PubMed=29507212;
RA Yadav V., Sun S., Billmyre R.B., Thimmappa B.C., Shea T., Lintner R.,
RA Bakkeren G., Cuomo C.A., Heitman J., Sanyal K.;
RT "RNAi is a critical determinant of centromere evolution in closely related
RT fungi.";
RL Proc. Natl. Acad. Sci. 115:3108-3113(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=4.1.1.49; Evidence={ECO:0000256|ARBA:ARBA00001389};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000256|ARBA:ARBA00006052}.
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DR EMBL; CP025766; KGB76990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095C8M4; -.
DR STRING; 294750.A0A095C8M4; -.
DR VEuPathDB; FungiDB:CNBG_2828; -.
DR HOGENOM; CLU_018247_2_0_1; -.
DR OMA; MRYAGEM; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000029445; Chromosome 8.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00484; PEPCK_ATP; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 1.
DR HAMAP; MF_00453; PEPCK_ATP; 1.
DR InterPro; IPR001272; PEP_carboxykinase_ATP.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR InterPro; IPR015994; PEPCK_ATP_CS.
DR NCBIfam; TIGR00224; pckA; 1.
DR PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Kinase {ECO:0000313|EMBL:KGB76990.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:KGB76990.1};
KW Transferase {ECO:0000313|EMBL:KGB76990.1}.
SQ SEQUENCE 551 AA; 61775 MW; A3A911A083CF79B4 CRC64;
MAPRQHQHDE FESNQFLGKE LKYFSQAGFD LDRIHIKRNA PVASLYEDAI LNEGAVISSN
GALINFSGKK TGRSPKDKRI VYEETSKDDV WWGPVNIKMD EHTFEINRER AIDYLNTREN
VYVFDGFAGW DPKYRIKVRI IASRAYHALF MHNMLIRPTP EELENFGEPD FIIYNAGQFP
ANRFTTGMTS TTSVGVNFKR MEMVILGTEY AGEMKKGIFS VMHYLQPVKF GQLSLHSSAN
QGIGKNDDVT LFFGLSGTGK TTLSADANRL LIGDDEHVWS DTGVFNIEGG CYAKCINLSA
EKEPEIFNAI KFGSILENVV YNPADRKPDY DDVSITENTR CAYPIEYIPN AKIPCIADRQ
PSNIIMLCCD AFGVLPPVSR LTPEQAQYHF VAGYTSKTPG TEDGIVEPSP TFSTCYGQPF
IILHPGRYAK MLAERMEKNR VNCWLINTGW TGGKFGTGKR CPLKYTRAIV DAIHNGSLAK
AEYENFPIFN LAIPKAVEGV PSDILNPEKV WPSKEAFKAE LDKLGGMFQK AFAKYEADID
EKVKLSGPVF A
//
