ID   CAPP_HAHCH              Reviewed;         881 AA.
AC   Q2SL23;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
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};
GN   OrderedLocusNames=HCH_01811;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000155; ABC28651.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2SL23; -.
DR   SMR; Q2SL23; -.
DR   STRING; 349521.HCH_01811; -.
DR   KEGG; hch:HCH_01811; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000000238; 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..881
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000082428"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        547
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   881 AA;  99332 MW;  19234A3B48790C07 CRC64;
     MMKELHPELR ENVRLLGELL GQSIRYHLGD EIFNKIEKIR IAAKADRNAE ISQRKQLKEV
     LSGLNDEELA PVARAFNQFL NLTNIAEQYH IVRRRAPASE LVDNRLDTIE VVFDRLIGQG
     VSKDKFFAQL ADLNLEFVLT AHPTEITRRT LIQKYDQISE CLESLDRSDL LDEEYAKIVE
     RLRRLITEAW HTDEIRYERP TAVDEAKWGF AVIENSLWQA VPDFMRQMDA ALLERFGEGL
     PINVNPVRFA SWMGGDRDGN PNVTSEVTRE VFLLSRWMAA DLYLRDIEAL RSELSMTACN
     GELARASGQS REPYRKILAK LRSRLEATRA WAAEALDSTK KPAAEVLLNN AELIEPLMVC
     YRSLRDCGME VIANGPLLDV IRRAQCFGLQ LVRLDIRQDS ERHSDVMKEI CAYLGIGDYS
     QWTEEEKQAF LIRELEGRRP LLPKEWPASA EAREVLDTCR VVAMQPPEGL ASYVISMASD
     PSDVLTVILL LRESGMRHHI PIAPLFETLS DLQGAADSIG RLLDLPWYRE YIGGKQEVMI
     GYSDSAKDAG QMAAAWAQYQ AQEALVKVAA KHDVKLTLFH GRGGTVGRGG GPANRAILSQ
     PPGSVAGNFR ITEQGEMIRF KFGQPKVAKQ SFNLYLGAVL EASLVPPPEP EPAWREMMDK
     LSHLAVNSYR EVVRERPGFV EYFRSATPEQ ELGKLALGSR PARRKASGGV ESLRAIPWIF
     AWTQMRLMLP AWLGSDTALQ TAVDDGGADT LKAMLTGWPF FETHVDMLEM VLSKVDPEIA
     RFYEERLVKP ELHPLGDELR RRAGCAVRLI NELKGQDELL LDNPVFMHSL QVRNPYTDPL
     HFLQVELLVR DRAEGETNKE TVEKALKVTM AGVAAGMRNT G
//