ID   H0PXQ6_9RHOO            Unreviewed;       915 AA.
AC   H0PXQ6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   ECO:0000313|EMBL:BAL23248.1};
GN   ORFNames=AZKH_0912 {ECO:0000313|EMBL:BAL23248.1};
OS   Azoarcus sp. KH32C.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL23248.1, ECO:0000313|Proteomes:UP000007106};
RN   [1] {ECO:0000313|EMBL:BAL23248.1, ECO:0000313|Proteomes:UP000007106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH32C {ECO:0000313|EMBL:BAL23248.1,
RC   ECO:0000313|Proteomes:UP000007106};
RA   Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA   Senoo K.;
RT   "Complete genome sequence of Azoarcus sp. KH32C.";
RL   Submitted (NOV-2011) 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, 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; AP012304; BAL23248.1; -; Genomic_DNA.
DR   RefSeq; WP_015434556.1; NC_020516.1.
DR   AlphaFoldDB; H0PXQ6; -.
DR   STRING; 748247.AZKH_0912; -.
DR   KEGG; aza:AZKH_0912; -.
DR   PATRIC; fig|748247.4.peg.912; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000007106; 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:BAL23248.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007106}.
FT   ACT_SITE        144
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        577
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   915 AA;  101361 MW;  DF23BCF426681A38 CRC64;
     MTQDKDAPLR EDIRLLGRVL GDTVRDQQGE AMFGLIERIR QTSVRFRRDD DRAARLELEG
     ILDALSREQT IQVVRAFSYF SHLANIAEDQ HHIRRTRAHL LAGSAPREGS LAHALARALD
     GRHTPGELAA FFDTAEVTPV LTAHPTEVQR KSILNCQTDI ARLLDQRDRM ALTPEERDDS
     DETLRSAVLT LWQTRMLRPA KLSVLDEVAN GLSYFDSTFL RELPRLYAHL EDQLAERDGA
     LGALELPAFL KVGSWIGGDR DGNPFVTAEV LERALALQAG LALGFYLDEL HALGARLSLA
     LGLVSASDAL LALAEHSPDH SPHRNDEPYR RAITGIYARL AATHRALLGI EPPRHPVAAA
     EPYASAAELA DDLDTIHRSL VANGSAALAR GRLRLLRRAV RVFGFHLAPI DLRQNSDVHE
     RVVAELLSTA RPEVDYRALG EEARCALLLE ELATPRPLAS PHVHYSEETE GELAIFRAAR
     TAHLRFGKAA ITNCIISKTD DVSDMLELAL LLKEAGLLRP HEQALDVNII PLFETIDDLA
     NAPSVMDRLF SLPGYMSLLG SRGQLQEVML GYSDSNKDGG FLTSGWSLYK AEIGLVEVFA
     RHNVRLRLFH GRGGSVGRGG GPSYQAILAQ PGGAVQGQIR LTEQGEVIAA KYGNPEVGRR
     NLEVLVAATL EASLLTDRSP APRADFLDTM QALSDAAFSA YRGLVYETEG FERYFWESTV
     ISEIAELNIG SRPASRKKGT RIEDLRAIPW VFSWAQCRLM LPGWFGFGSA VKAWRAANPD
     DGLARLQAMY KEWSFFATLL SNMDMVLAKS DLAIASRYAG LVKDAKLREE IFNRIRTEWQ
     DTVDALLAIT GQTELLDDNP LLKRSIRNRF PYLDPLNHVQ VELLRRHRES HEDARIRLGI
     HLSINGIAAG LRNSG
//