ID A0A167ASV5_9GAMM Unreviewed; 948 AA.
AC A0A167ASV5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ECTOBSL9_1907 {ECO:0000313|EMBL:ANB02495.1};
OS Ectothiorhodospira sp. BSL-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=1442136 {ECO:0000313|EMBL:ANB02495.1, ECO:0000313|Proteomes:UP000076772};
RN [1] {ECO:0000313|EMBL:ANB02495.1, ECO:0000313|Proteomes:UP000076772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSL-9 {ECO:0000313|EMBL:ANB02495.1,
RC ECO:0000313|Proteomes:UP000076772};
RA Saltikov C., Conrad A., Hernandez J., Stoneburner B., Oremland R.,
RA Rosen M., Miller L., McCann-Hoeft S., Pourmand N., Bernick D.;
RT "The arx anaerobic arsenite-oxidization pathway is conserved in Halomonas
RT and Ectothiorhodospira strains isolated from Big Soda Lake, Nevada.";
RL Submitted (JUN-2015) 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,
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}.
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DR EMBL; CP011994; ANB02495.1; -; Genomic_DNA.
DR RefSeq; WP_063464840.1; NZ_CP011994.1.
DR AlphaFoldDB; A0A167ASV5; -.
DR STRING; 1442136.ECTOBSL9_1907; -.
DR KEGG; ebs:ECTOBSL9_1907; -.
DR PATRIC; fig|1442136.6.peg.1948; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000076772; 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:SF46; 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:ANB02495.1}.
FT ACT_SITE 153
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 604
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 948 AA; 107351 MW; 013A71F5DE38DCCF CRC64;
MTQQPDRVQD SSTGDKPLRA RVKLFGKLLG NIIRRLEGPE VFRAVETLRR GFVSLRQQDD
PDKRARLMRL IDELDPKRLE TIIRAFSIYF SLANLAEEDF LYRERRRQVT RGGPLWLGSF
DHTVREFKAA EVSAEQLQFL LEQVKYMPVF TAHPTEARRR TVMEAQRRIF LAAEPLNKGR
IGREERREVI RQLETQIQVL WRTNEVRVTK PEVLDEIKYG LFYYEESLFT AVPLAYRLLE
KAIRRTYGTD EAGRPNVRIP SLLRFGSWIG GDRDGNPYVT PAVTEKACRL AMEQVLSEYL
RRVHDLRFVL THSSLMCQPT RALMDSLAED DSISSAVFRE GLNEMRTEPY RRKLYFIRHR
LSETLNTVRR RLAGETAVLP VQSAYHGPEE LLRDLYVIRD SLESHGDGNI AGADLTDLIR
LVETFGFHLH HLDMRQESLV HTAAVAEILA STGDEADYDA QDESTRLALL GRLLTRDDFT
CDTEALSEET RQTLAVFQTM ARLRGEVGGD GIGTYVISMT HAASHVMEVM LLAQLAELAR
LGPGEEFEAD VCHVRVSPLF ETIEDLHHVE SVLESLLGDP VYARLLKASG NRQEVMLGYS
DSCKDGGILA SAWNLYDAQR KIIDITEAHG VECRLFHGRG GTIGRGGGPT HESIMAQPPG
TVQGEIKFTE QGEVLSYKYS NVETAVYELS IGATGLIKAS RGLIGQGSQD NPDFLGVMNA
LAEHGEQAYR GLTDHTSGLL DYFYEATPVE EIGRMNIGSR PSHRRKADRS KSSIRAIPWV
FGWAQSRHTV PAWYGIGTAL ETWHGDDPER LAQLQSMYRE WPFFHSLLSN CQMSLAKADM
GIAEEYAELC QDREQAQQIY QVIRDEYQRT VAQVLAVSGT RSLLEENPRL ALSLTRRDPY
LDPLNHIQII LLRRYRALHA QGEKAEDPWI SPLLRSINAI AAGMRNTG
//
