ID A0A154R4C2_9GAMM Unreviewed; 901 AA.
AC A0A154R4C2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=RhoFW510R10_09790 {ECO:0000313|EMBL:KZC33016.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC33016.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC33016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC33016.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZC33016.1}.
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DR EMBL; LVJU01000015; KZC33016.1; -; Genomic_DNA.
DR RefSeq; WP_068090165.1; NZ_LVJU01000015.1.
DR AlphaFoldDB; A0A154R4C2; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000076310; Unassembled WGS sequence.
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:KZC33016.1}.
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 568
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 901 AA; 99575 MW; EA1E4F7BCCDF2FD3 CRC64;
MESSREPEFL PPDGPLREDV SRLGAMVGRM LAEQGGDVFF ERVEQVRTAA IRRRREGASV
EELAASLAGL DAHDAEALAR AFATYFQAVN TAERVHRIRR RRDYQREGST PQPESLLDVL
GRLKAEGVGA DELVGWLERL WIEPVFTAHP TEAVRRSLLE KEQAIVASLI DGFDQQRTPQ
ERREDDDRIY MALSAGWQTA EASPVRPSVQ DEREHVDFYL ANPLYRIVPA LYESLAQALQ
RTYGVAIRLP RLLRFASWVG GDMDGNPNVG ADTIAACLDS QRALVLERYR EDVAALARLL
SQTEGRVAVS AALRARLADY RERFPAAAAL IRPRHADMPY RCLLQLVGAR LALTRDDGPD
GYASSSGLLD DLQLIADSLF QHHGVHAGAY AVERLLCRVR SFGFHLARLD VRQDSRVHDD
ALAALLADPD WAMRDGAARA DRLRPYACGE AAFPHSSDAN AASLQAVFAT LRDSRASHGE
DATGLYIISM ARSAADVLAV LALARRGGLV DQANDVPLNI APLFETVDDL NNAPATLRAL
LDDPVYRRHL AARGDQQWVM LGYSDSGKDG GTLASRWGLQ RAQAALLEVA HAAGIQLAFF
HGRGGSASRG GARITPALMS APRGAVAGVL RVTEQGEVIH RKYGIRALAL RNLEQTVGAV
LRASLRPPGG EPRVERWCTL MDALSATSRR HYRAFVERER FVDYFRSATP VDVIERMTLG
SRPASRRSMR GVQDLRAIPW VFAWTQCRTI LPGWYGLGSA LEQGVQQFGE AALAEMARDW
PFFCNLLDDV EMVLAKCDLH IAEAFSKLSG PLHDEFFGLI RAEFARTRHW LLRLKGSEVL
LRGEPRLAAS IRLRNPYVDP MSLLQVDLLQ RWRASDRQDD AVLQALVACV NGVSQGLQNT
G
//