CAPP_MYCA1
ID CAPP_MYCA1 Reviewed; 935 AA.
AC A0QHY0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=MAV_3336;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-Rule:MF_00595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
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DR EMBL; CP000479; ABK67960.1; -; Genomic_DNA.
DR RefSeq; WP_011725407.1; NC_008595.1.
DR AlphaFoldDB; A0QHY0; -.
DR SMR; A0QHY0; -.
DR EnsemblBacteria; ABK67960; ABK67960; MAV_3336.
DR KEGG; mav:MAV_3336; -.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 398146at2; -.
DR Proteomes; UP000001574; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR HAMAP; MF_00595; PEPcase_type1; 1.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR022805; PEP_COase_bac/pln-type.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR033129; PEPCASE_His_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium.
FT CHAIN 1..935
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000025565"
FT ACT_SITE 161
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 593
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 935 AA; 102548 MW; DF4E7779B3A41F2B CRC64;
MVEASEGTLE PIGAVQRTLV GREATEPMRA DIGLLGAILG DTVREQNGQQ VFELVERARV
ESFRVRRSEI DRAELARMFA GIDIHQAIPV IRAFSHFALL ANVAEDIHRE RRRAIHVAAG
EPPQDSSLAA TYAKLDRAQL DSATVAEALR GAVVSPVITA HPTETRRRTV FVTQHRITEL
MRLHAEGHIE TDDGRNIELE LRRQVLTLWQ TALIRLSRLQ ITDEIEVGLR YYAAAFFKVI
PRVNAEVRNA LRARWPGADL LDEPIVAPGS WIGGDRDGNP NVTADVVRRA TGDAAYTALA
HYLAELTACE QELSMSARLV AVTPELAALA EDCAEKARAD EPYRRALRVI RGRLTATAAE
ILDRRPQHEL DLGLPPYATP AELRGDLDTV DASLRAHGSA LLADDRLALL REGVRVFGFH
LCGLDMRQNS DVHEEVVAEL LAWAGVHPDY RSLPEDERVE LLAAELGTRR PLVGDRAELS
ELADKELGVV RAAAHAIRRY GPAAVPNYVI SMCRSVSDVL EAAILLKEAG LIDASGPEPY
CPVGISPLFE TIEDLHNGAA ILHAMLELPL YRALVAARGQ SQEVMLGYSD SNKDGGYLAS
SWAVYRAELA LVEVARKTGI RLRLFHGRGG TVGRGGGPSY EAILAQPPGA VNGSLRLTEQ
GEVIAAKYAE PQVAQRNLES LVAATLESTL LDVEGLGDTA EPAYAVLDEV AVLAQRAYAE
LVHETPGFVD YFMASTPVSE IGSLNIGSRP TSRKPTESIA DLRAIPWVLA WSQSRVMLPG
WYGTGSAFEQ WIAAGPQSRA ERVDILHDLY RRWPFFRSVL SNLAQVLAKS DLGLAAQYAE
LVDDAALRRR VFGKIADEHR RTIAMHKLIT GQDNLLADNP ALARSVFNRF PYLEPLNHLQ
VELLRRYRSG DDDELVQRGI LLTMNGLTSA LRNSG