ID   D1AY04_STRM9            Unreviewed;       884 AA.
AC   D1AY04;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=Smon_0707 {ECO:0000313|EMBL:ACZ01180.1};
OS   Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS   9901).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Streptobacillus.
OX   NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ01180.1, ECO:0000313|Proteomes:UP000002072};
RN   [1] {ECO:0000313|EMBL:ACZ01180.1, ECO:0000313|Proteomes:UP000002072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC   {ECO:0000313|Proteomes:UP000002072};
RX   PubMed=21304670; DOI=10.4056/sigs.48727;
RA   Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA   Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA   Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA   Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Chain P.;
RT   "Complete genome sequence of Streptobacillus moniliformis type strain
RT   (9901T).";
RL   Stand. Genomic Sci. 1:300-307(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;
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; CP001779; ACZ01180.1; -; Genomic_DNA.
DR   RefSeq; WP_012858731.1; NC_013515.1.
DR   AlphaFoldDB; D1AY04; -.
DR   STRING; 519441.Smon_0707; -.
DR   GeneID; 29674073; -.
DR   KEGG; smf:Smon_0707; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002072; 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   Reference proteome {ECO:0000313|Proteomes:UP000002072}.
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        550
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   884 AA;  102215 MW;  843AA6C586A65987 CRC64;
     MDSVILKPDD EIKLNKEWIS KEINIVKNIL SEIVPDIDID SILDNEKHFK DIEKINPDVV
     RVLTILPLLI NIVEDVYQSK ILKYNTITKN YTEGMLDNLL YKLDLNNMNK ENLTEIFSNI
     RVVPVLTAHP TQVQRKSILD LTQNIYEILE KRELVEHNLL DENEWMNELR KNINLLWRTD
     ILRSSKLRVG NEITNSLSYY DSTFLKAIPK INIKFKEIAK KLGIFSNSYT PILMGTWIGG
     DRDGNPFVTE ETLLNAAYSQ FETAIEYYIS ELKKLYREFS ISSLKNEYSD ELKELEKLSK
     DNLEHRTYEP YRLVISYIID NLQDVKVKLL KEKLELPYDS YYNSKKLLND LLAIRKSIKL
     YSDEIIAYGR LDELIESVKV FGYHLSSIDL RQDSSVYEFC VNELLNIAKI TDNYSALTEE
     EKCEILINQI ENEPRKLSSV NCKKSEILEK ELSIFSTMKK LINIFGKNII EQNIISHTVE
     ISDMLELALL LKEFDLDGKV NISPLFESIE DLKNSEKIMK TWFELDILKK WMSNNGSLQE
     IMLGYSDSNK DGGYITSSWH LYKAQKELVS LAQKYGVKLN FFHGRGGTVG RGGGPSYEAI
     LSQPSESILG KIRLTEQGEV IGAKYGNLDL GKFNLEALLS ATLEKSLKDD TKDIKEYENI
     MEQISNISYE KYRNLVYETE GFSEYFFEST PINEVSSLNI GSRPSSRKKV LDIEGLRAIP
     WVFSWSQIRV MLPGWYGVGT SFNKWIKENN GLETLKLMYR NWPFFKALLS NLEMVLSKTD
     MNIAKEYAKL VKNENLSTKI FNMINDEWIL TFNLLKEITG INYLLEDNEM LTLSLKNRLP
     YFNALNYLQI ELIKQQRAGN NTEEINKAIH TTINGIATGL RNSG
//