ID   CAPP_AZOC5              Reviewed;         931 AA.
AC   A8I060;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=AZC_4669;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) 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; AP009384; BAF90667.1; -; Genomic_DNA.
DR   RefSeq; WP_012173188.1; NC_009937.1.
DR   AlphaFoldDB; A8I060; -.
DR   SMR; A8I060; -.
DR   STRING; 438753.AZC_4669; -.
DR   KEGG; azc:AZC_4669; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   Proteomes; UP000000270; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..931
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000072621"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   931 AA;  102788 MW;  94A775227B24E960 CRC64;
     MTSAVWAVVS EQEAGGPDKD QPLRDDIRLL GRILGDTVRE QEGDAIYELV ETIRQTSIRF
     HRDADEAARQ ELNALLESMT PEVAVQIIRA FSYFSHLANI AEDQHHSRRN RAHAVAGSAP
     RPGTLANALA RAEKAGIGAA ELRAFFDAAL VSPVLTAHPT EVRRKSTMNR EMEIADLLDL
     KERLQATPQE AREQDEKLRR AVLTLWQTAL LRKFKLTVLD EVQNGLSYYD YTFLAEVPRL
     LCALEDHLAE QEGGEPGAEL PPFLRIGSWI GGDRDGNPFV TADVLRETVR QHRDRVMAFY
     LEQVGLLVTE LSLAKRLVAV SEDLTALAER SGDRAPEHRE EPYRLALVGI HNRLKATVAA
     QKAADDGKTM GAAEDGHLPY PDAAAFRADL DILYRSLMAN GSAILARGRL RHVRRAVDSF
     GFHLASLDLR QNSDVHERTV ADLLEQAAPG TNYHALDEEA RIAVLRAELT NPRPLASPFL
     SYTEETRSEL AILRTAAEAH ARLGKTVIPN AIISKAEGIS DMLELALLLK EVGLVSATGE
     SAINVIPLFE TIGDLQACGP VMDRLLALPE YRALVDSRGG EQEVMLGYSD SNKDGGFVSS
     GWELYKAEIA LIEVFARHKV KLRLFHGRGG SVGRGGGPSY DAILAQPAGA VSGQIRITEQ
     GEIISSKYSN PENGRRNLEI LVSATLESTL LEAEQASPRP EFLAAMEELS KTAFTAYRSL
     VYETPGFEDY FWSSTVISEI ATLNIGSRPA SRNKTRAIEA LRAIPWVFSW SQCRLMLPGW
     YGFGTAIAAF VEARPVDGIA FLQSMYREWP FFRTLLSNMD MVLSKSSLAV ASRYAELVPD
     EELRTRIFSR ISAEYQSAIT SLLAIMGQKK LLEANPLLDR SIRNRFPYLD PLNHIQVELL
     KLHRSDAGSD HVLHGIQLTI NGISAGLRNS G
//