ID B0BZ90_ACAM1 Unreviewed; 1012 AA.
AC B0BZ90;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 89.
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,
CC ECO:0000256|HAMAP-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; 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 OMA; PWVFGWT; -.
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
//