ID   J9YVY3_9PROT            Unreviewed;       894 AA.
AC   J9YVY3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
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   ORFNames=HIMB5_00003710 {ECO:0000313|EMBL:AFS47140.1};
OS   alpha proteobacterium HIMB5.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=859653 {ECO:0000313|EMBL:AFS47140.1, ECO:0000313|Proteomes:UP000006098};
RN   [1] {ECO:0000313|EMBL:AFS47140.1, ECO:0000313|Proteomes:UP000006098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB5 {ECO:0000313|EMBL:AFS47140.1,
RC   ECO:0000313|Proteomes:UP000006098};
RA   Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA   Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA   Friedman R., Venter J.C.;
RL   Submitted (SEP-2012) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003809; AFS47140.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9YVY3; -.
DR   STRING; 859653.HIMB5_00003710; -.
DR   KEGG; apm:HIMB5_00003710; -.
DR   PATRIC; fig|859653.3.peg.366; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006098; 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:AFS47140.1}.
FT   REGION          596..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        559
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   894 AA;  104022 MW;  9B62E6CDD48A01AE CRC64;
     MKKRDLYYDR IPTKFLREDI RLLGKILGDV LKEQEGGKFF KLVEDIRLLS KPSLNNYGSK
     NPHDRLSNKI KNLNSETIFK LTRAFNHFCN LMNLAEAHDT SHTLNEIEQN KNKKTKSLFI
     EEIFKNFFKN KLIPNKKIYD LAQNLKIGVV LTAHPTEVKR RTLIQKYANL IELLEQRYLY
     KNFQKKINEI DKALYSEITI IWKTDDIKRS KPSPLDEARW GLAIIEDSLW DTIPRVYKRL
     NKIFKKNYGK DLPRSFNPIE FGSWMGGDRD GNPNVTSKVT EKVILFSRWQ AAKLYERELT
     KLIQDLSMQN CSSKIKKISK NSFEPYRVYL RPIRDKIRST YINIEEHLNK NKKLNNDLLF
     KDKYELINVL RDVRKSLNEN NDKRIGNSVL LDLLRRARCF GINLAKLDIR QESSRHSLLV
     SEILRNNLRI KFENFDENKK VQLLSKLITD KKGLKNLKLK NKLNKEVWNT FEVISKQPIE
     CLGAYVISMT SSSSDILNVY YLQKLAKISQ PLRVVPLLET LDDLKNGKKI MEKLFSLSWY
     RKLIKNKQEV MIGYSDSSKD AGKLSSSWNQ YKVEEELRNI AKKYKISLTF FHGRGGSPGR
     GGGPIQSTLK SQPSNTVNGK IRITDQGEVI QQKYGYKPLA EYNLCSYIGS VMEATLNPPP
     KSKPQWRSLI ERMTELSTAS YRRSINANEE FIRYFKTVTP HKALGKLSIG SRPTKRKNVD
     NIQSLRAIPW VFAWTQIRLL LPAWLGTSEA LRYAGIKKFK NVLNDMQINW PFFSSTMDIL
     DMVISKVDPE ISIIYENNLA DDKLRRVGKK LRFQFDQLVK LHKKITPKEI LNERKKFRKS
     LYVRNNYTEV LNVLQAKIMG KLNSKKLSNL DRKFLEDALM TSIAGISAAI KNTG
//