ID A0A172UPD0_9MYCO Unreviewed; 931 AA.
AC A0A172UPD0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN ORFNames=A7U43_17575 {ECO:0000313|EMBL:ANE80866.1};
OS Mycobacterium adipatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE80866.1, ECO:0000313|Proteomes:UP000077143};
RN [1] {ECO:0000313|EMBL:ANE80866.1, ECO:0000313|Proteomes:UP000077143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE80866.1,
RC ECO:0000313|Proteomes:UP000077143};
RA Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT sp. YC-RL4.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00595};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR EMBL; CP015596; ANE80866.1; -; Genomic_DNA.
DR RefSeq; WP_067997867.1; NZ_CP015596.1.
DR AlphaFoldDB; A0A172UPD0; -.
DR STRING; 1682113.A7U43_17575; -.
DR KEGG; madi:A7U43_17575; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000077143; 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 Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00595};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW Pyruvate {ECO:0000313|EMBL:ANE80866.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077143}.
FT ACT_SITE 161
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 593
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 931 AA; 101949 MW; C379F546F9FEDC2D CRC64;
MADGPDTALA PMGSVYRTQV GREATEPMRE DIRLLGAILG DTVRDQNGDG VFDLVERARV
ESFRVRRSEI DRAELAGLFR DIDVHQAIPV IRAFTHFALL ANVAEDIHRE RRRAVHEAAG
EPPQDSSLAA TYRKLDHAQL DAGAVADALT GALVSPVITA HPTETRRRTV FDTQHHITEL
MRLRLHGQTR TDNGRDIETE LRRHILTLWQ TALVRLSRLK ISDEIETGLR YYPAAFLDVI
PRVNAEVRTA LQERFPGTAL LAEPILRPGS WIGGDRDGNP NVTADVVRLA TGRAAFTAFA
HYFGEITALE EELSMSARLV RVSAGLEALA DACAEPARSD EPYRRALRVV HARLTATAAR
VLDRQPEHEL DLGLPAYDTP AQLLEDLDVV DESLRANGSA VLADDRLARL REAVRVFGFH
LSGLDMRQNS EVHEQVIAEL LAWAGVHPDY ASLPEDERVT LLAKEIGTRR PLIGPGADLS
ELAAKELGIV AAAARAVQVF GREAVPNYII SMCQSVSDML EAAVLLKEAG LLDVSGAQPY
APVGIVPLFE TIDDLQRGSS ILEAALDVPV YAAAVAARNG HQEVMLGYSD SNKDGGYLAA
NWALYRAELE LVESARKTGI RLRLFHGRGG TVGRGGGPSY DAILAQPPGA VKGSLRITEQ
GEVIAAKYAE PRIAHRNLET LLAATLESTL LDTEGLGDLA DSAYAVLDDL AARAQRAYAE
LVHETPGFVE YFKESTPVSE IGALNIGSRP TSRKPTTAIS DLRAIPWVLA WSQSRVMLPG
WYGTGAAFEQ YVGGDDAKLE VLRDLYRRWP FFRTVLSNMA QVLAKSDLGL AARYSELVAD
EDLRARVFDK IAAEHERTVR MHGLVTGQDD LLADNPALAR SVFNRFPYLE PLNHLQVELL
RRFRSGEQDE LVQRGILLTM SGLASALRNS G
//
