ID   D3PZ06_STANL            Unreviewed;       914 AA.
AC   D3PZ06;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
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   OrderedLocusNames=Snas_5805 {ECO:0000313|EMBL:ADD45435.1};
OS   Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS   NBRC 102104 / LLR-40K-21).
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Stackebrandtia.
OX   NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD45435.1, ECO:0000313|Proteomes:UP000000844};
RN   [1] {ECO:0000313|EMBL:ADD45435.1, ECO:0000313|Proteomes:UP000000844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC   LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX   PubMed=21304662; DOI=10.4056/sigs.47643;
RA   Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA   Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT   40K-21).";
RL   Stand. Genomic Sci. 1:292-299(2009).
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; Evidence={ECO:0000256|HAMAP-
CC         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; CP001778; ADD45435.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3PZ06; -.
DR   STRING; 446470.Snas_5805; -.
DR   KEGG; sna:Snas_5805; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000000844; 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; 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.
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:ADD45435.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000844}.
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        576
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   914 AA;  100376 MW;  4BA98DF84CEA815E CRC64;
     MDTTLEDDDA GLRADIRRLG SLLGDSLVRQ EGQQLLDLVE EIRHLVRTDA KAAAQRLAEL
     SVDTGMNLAR AFALYFHLAN ITEQVHRARE LRRRRVRRGG WLEEAATEIK AEGLDADRIA
     KAARGLEVSP VFTAHPTEAA RRSILTKLRQ LADVLDSEAA EAALAGQADT AATDLRLAEL
     IDLLWQTDEV RINRPEPTDE ARNAVYYLTD LYADAAPRVL RDLAQVLTEL GAEPSLSDSP
     LRFGTWIGGD RDGNPNVTPE VTRRVLTLQH EHGIRAAESM VESMISELSV SQQLRPATPE
     FMASLEADLA ALPELPPRFR RVNSAEPYRL KARCVRAKLA ATRARHASGT AHVPGRDYAD
     GTELYTDLET FYDSLTASTG GLAAEGRLAD SMRVVAAFGL HLATMDIREH AAKHHAALAE
     LFDRLRPDDD LDKPYGDLSR AERFALLAAE LDSRRPLLTP AAALSPETRK TLDVFRCIVS
     AQRRFGPQVA ATYIVSMTQG PDDLLAAAVL AREAGLVDIH AGRADIGFVP LLEGVPELEA
     GRQIWNDLLN TPAYRRIVDA RGGIQEVMLG YSDSNKESGI AASQWAIQSA QRELRDAAAE
     HGVRLRLFHG RGGTVGRGGG PTHEAILAQP YGTLDGTIKV TEQGEVLSDK YTLPVLAREN
     LELTVAAVLK ATLLHDTPRH DASTLDVWYG TMDRLSGSAR TAYRSLIDHP GLPEYFWAVS
     PTELLGALNI GSRPAKRPDA SAGLDGLRAI PWVFGWTQSR QIVPGWFGVG TGLATAREAV
     SDEVLSAMYE RWQFFSTFIS NVEMTLVKTD MDIAERYVDT LVPPRLRPLF DTIRAEHART
     VTEVLRLTGK SELLADNPQL RRTLAVRDRY LAPLHHLQIA LLHRHRESAT DDPSLTRALL
     TTVNGIAAGM RNTG
//