ID   Q1QJX7_NITHX            Unreviewed;       929 AA.
AC   Q1QJX7;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=Nham_2691 {ECO:0000313|EMBL:ABE63470.1};
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE63470.1, ECO:0000313|Proteomes:UP000001953};
RN   [1] {ECO:0000313|EMBL:ABE63470.1, ECO:0000313|Proteomes:UP000001953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14
RC   {ECO:0000313|Proteomes:UP000001953};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) 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; CP000319; ABE63470.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1QJX7; -.
DR   STRING; 323097.Nham_2691; -.
DR   KEGG; nha:Nham_2691; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001953; 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:ABE63470.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001953}.
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        591
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   929 AA;  103363 MW;  99B0C657833A82DF CRC64;
     MSRQMMPLPR AGQPESDAAA LDARLRDDIR LLGRILGDTV RDQEGAAVFD LVERIRQTSI
     RFHRDEDKPA RRELEAILDG MSTDETVLVV RAFSYFSHLA NIAEDQNNIR QMRSQSLEGG
     ARHEGVLAHT LACAREAGFS GAELQAFFDS ALVSPVLTAH PTEVRRKSTI DREMEVAFLL
     DRRERMQLTP DEYEVSEEQL RRAVLTLWQT NLLRRTKLTV LDEVANGLSF YDYAFLREVP
     RLHCVLEDRL QDASADGASN EMASFLRIGS WIGGDRDGNP FVTADVMRGT LRMQASRVLR
     YYLDELHELG RELSLAADLT DVSPELRGLA ERSADTSPHR RGEPYRLAVS GIYARLSATA
     LKLKADTLRP PYGKAPPYAS AAEFSADLDV LHRSLTQNNS EVIARGRLRH LRRAADCFGF
     HLACLDLRQN STVHERTIAE LLDAAVPGTS YLALSEEARI VVLLRELRSA RPLTSPFITY
     SDETLGELAV FHAAAEAHEM FGPGAIPQCI ISMSEGVSDL LEVALLLKEA DLVDPTGHSA
     INIVPLFETI EDLQACAGIM DRLLSLPEYR ALVDSRGGLQ EVMLGYSDSN KDGGFVTSGW
     ELYKAEIGLV EVFERHQVRL RLFHGRGGSV GRGGGPSYDA ILAQPGGAVN GQIRITEQGE
     IISSKYSNAE VGRNNLEILA AATLEASLLQ PRQSAPSLDY LDAMESLSSR AFAAYRNLVY
     ETPGFEDYFW ASTVINEIST LNIGSRPASR KKTRRIEDLR AIPWVFSWAQ CRVMLPGWYG
     FGSAVESWIA DHPDKGMAFL QELYGEWPFF RMLLSNMDMV LAKSSIAIAS RYADLVPDVT
     LRETIFGRIR SEWHLTIDTL LAIMGQERLL AGNPLLERSI RNRFPYLDPL NHVQVELLKD
     HRAQGGDEQV LRGIQLTING ISAGLRNSG
//