ID   B1WNZ1_CROS5            Unreviewed;      1020 AA.
AC   B1WNZ1;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   ECO:0000313|EMBL:ACB53170.1};
GN   OrderedLocusNames=cce_3822 {ECO:0000313|EMBL:ACB53170.1};
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB53170.1, ECO:0000313|Proteomes:UP000001203};
RN   [1] {ECO:0000313|EMBL:ACB53170.1, ECO:0000313|Proteomes:UP000001203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68 {ECO:0000313|Proteomes:UP000001203};
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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; CP000806; ACB53170.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1WNZ1; -.
DR   STRING; 43989.cce_3822; -.
DR   KEGG; cyt:cce_3822; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000001203; Chromosome circular.
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:UP000001203}.
FT   REGION          119..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        667
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1020 AA;  117283 MW;  3BAACD5E8385A87C CRC64;
     MLLVMLLESL QSTVEEVNIF STSDLFLRQR LKLVESLWES VLKAECGQEL VDLLEKLRKI
     CSPEGQVTDK PKTSINELIE GLELNEAIRA ARAFALYFQL INIVEQHYEQ RDQQLNRRAT
     YQESEKARNN HAKEENKANG SVGADLLEKA LVGGTENQEK GGTFHWLFPQ LKRLNVPPQQ
     IQRLLEQLDI RLVFTAHPTE IVRHTIRLKQ RRIATLLRRL DYAEESFRGM GLSSSWEAES
     IIEQLNEEIR LWWRTDELHQ FKPSVLDEVD YTLHYFDEVL CDALPQLSQR LQQALKANFP
     RIKPPHNTFC RFGSWVGGDR DGNPFVTPEV TWRTACYQRN LILEKYLAAI EDLTEILSSS
     LHWSNVSQDL LDSLERDRVA MPEIYDELAI RYRQEPYRLK LAYIEKRLET TRDRNNHLAN
     PEKRQILTEE TPPNIYHSGE EFEAELQLIK RNLEETGLKC QALENLIFQA QMFGFTLTQL
     DFRQESSRHS ETIEVIANYL NVLPRPYGEL SETEKVNWLV GELQTRRPLI PMEMPFDEKT
     IETIETMRML RYLQQEFGVE ICQTYIISMT NDVSDVLEVL LLAKEAGLYD PGTSTTTIRI
     VPLFETVDDL KRAPEIMDAL FKLTLYRAAL AGGYDYLDEA KKEQLPPPEL QPANLQEIMV
     GYSDSNKDSG FLSSNWEIHK AQKSLQKVAE PYGLALRLFH GRGGSVGRGG GPAYAAILAQ
     PTGTINGRIK ITEQGEVLAS KYSLPELALY NLETATTAVI QASLLGSGFD DIVPWNDIME
     ELASSARKAY RSLIYEQPDF LDFFLSVTPI PEISQLQISS RPARRKSGKK DLSTLRAIPW
     VFSWTQSRFL LPAWYGVGTA LESFLQQEPN ENLKLLRYFY LKWPFFKMVI SKVEMTLSKV
     DLQIAHHYVK ELSQPEDIER FNKVFERISQ EYHRTRDIIL SINEQPKLLE GDAGLQRSVQ
     LRNGTIVPLG FLQVSLLKRL RQYTRQAESG VIHFRYSKEE LLRGALLTIN GIAAGMRNTG
//