ID   B0BZ90_ACAM1            Unreviewed;      1012 AA.
AC   B0BZ90;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 90.
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:ABW29534.1};
GN   OrderedLocusNames=AM1_4560 {ECO:0000313|EMBL:ABW29534.1};
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC   Acaryochloridaceae; Acaryochloris.
OX   NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW29534.1, ECO:0000313|Proteomes:UP000000268};
RN   [1] {ECO:0000313|EMBL:ABW29534.1, ECO:0000313|Proteomes:UP000000268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(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; CP000828; ABW29534.1; -; Genomic_DNA.
DR   RefSeq; WP_012164844.1; NC_009925.1.
DR   AlphaFoldDB; B0BZ90; -.
DR   STRING; 329726.AM1_4560; -.
DR   KEGG; amr:AM1_4560; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000268; 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:ABW29534.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000268}.
FT   ACT_SITE        194
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        658
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1012 AA;  116155 MW;  B5522759E3A86FC2 CRC64;
     MRSTLNRNHP QLVQPNRLES LLLHRIKVIE DLLEGVLRDE CGQELVDLLR QLRSMCSPEG
     QAPTVPETEV LKVVEKLELD EAIRAARAFA LYFQLINIVE QHYEQEESIV RTRGAITSSP
     VALPNVGGSA ERAENHANGQ TELPEHSIFD AILREPNAGT FTWLFPKLKQ LNVPPRHIQN
     IIQNLDIQLV FTAHPTEIVR QTIRAKQRRI AKILGKLDEA EAGLANNTRS NWEVDALQAQ
     LTEEVRFWWR TDELHQFRPT VLDEVEYSLH YFREVLFDAI PQLYHRLSLN LKQAFPKLQP
     PRYNFCKFGS WVGSDRDGNP AVTPDITWQT SCYQRNLVLE KYIQSVNKLI NLLTLSQYWS
     EVPPGLEKSL GQDQLQMPEV YDRLSIRFLG EPFRFKLSYI LKRLENTRDR NQQQAQLIDF
     SHPIHPQGMN EQIYYPAAQN FLAELRVVQE NLQATGINCQ ELDTLIGQVE IFGFNLTQLD
     IRQESSCHSD ALTEIVNYLQ ILPKPYNELS ESERLEWLTQ ELQTRRPLIP HDLPFSDKTQ
     ELINTFRMIR RLQEEFGVEI CRTYIISMSH DASDLLEVLL LAKESGLFDP TTASGTLHVI
     PLFETVDDLQ RAPGVMTQLF DLTFYRNYLV DAQASQEPSS NPPLSLQEIM LGYSDSNKDS
     GFLSSNWEIY KAQQRLQETA EPYGVSLRIF HGRGGSVGRG GGPAYEAILA QPGYSVNGRI
     KITEQGEVVA SKYSLPELAL YNLETISTAV IQSSLLRSTM DSIEPWHEIM EDLSARSRKR
     YRALIHEQED LVDFFYEVTP INEISQLQHA ARPARRRADN RRTLEGLRAI PWVFSWTQSR
     FLLPAWYGVG TALQDFLDEK SAEHLTLLQY FYGKWPFFKM VISKVEMTLA KVDLQIAHHY
     LQELTSSEDV DRFERLFEQI AQEYYLTREM VSKITGNQQL LDGDPNLKRS VHLRNGTIVP
     LGFLQVSLLK RLRQHQRQDR VALGAGNVSE KDLLRGALLT INGIAAGMRN TG
//