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Database: UniProt
Entry: A0A154R4C2_9GAMM
LinkDB: A0A154R4C2_9GAMM
Original site: A0A154R4C2_9GAMM 
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
//
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