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Entry: D3SCN8_THISK
LinkDB: D3SCN8_THISK
Original site: D3SCN8_THISK 
ID   D3SCN8_THISK            Unreviewed;       946 AA.
AC   D3SCN8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-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   OrderedLocusNames=TK90_2121 {ECO:0000313|EMBL:ADC72611.1};
OS   Thioalkalivibrio sp. (strain K90mix).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC72611.1, ECO:0000313|Proteomes:UP000009099};
RN   [1] {ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT   "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADC72611.1, ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|EMBL:ADC72611.1,
RC   ECO:0000313|Proteomes:UP000009099};
RX   PubMed=22675584; DOI=10.4056/sigs.2315092;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Foster B., Sun H.,
RA   Ivanova N., Pati A., D'haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of Thioalkalivibrio sp. K90mix.";
RL   Stand. Genomic Sci. 5:341-355(2011).
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; CP001905; ADC72611.1; -; Genomic_DNA.
DR   RefSeq; WP_012983484.1; NC_013889.1.
DR   AlphaFoldDB; D3SCN8; -.
DR   STRING; 396595.TK90_2121; -.
DR   KEGG; tkm:TK90_2121; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000009099; 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}.
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   946 AA;  107724 MW;  2FCD4D8B2C9B2471 CRC64;
     MTQTDLDDRF LPKDKELRAR VRLFGELLGN VIRKLEGQTV FDAVEKLRRG FVSLRKDEDP
     QLRQRLMADI THFDAALTER VIRAFSIYFS LVNIAEEDLF YRWRRAQVSS GEPLWTGSFD
     QTLRELHNEG VTAAELERLL AELHYQPVFT AHPTEARRRT TMENQRRVFE TADRLNQPEL
     GEEERRLIIE ELETQIQLLW RTNEVRVKKP QVQDEIKYGL FYFEESLFEA IPQSYRFLEK
     AIRRIYGVHP DGSLPVRIPA FLHFGSWIGG DRDGNPNVTP EVTELACRLA MEQVLREYIK
     RVNHLRNVLT HSAYMCQPSQ EFLDSLDADS NIANAVFHGA SDRFESEPYR RKLYIMRYRL
     RETLETVCRR IQGEAAVLPT NSAYADADAF LQDLNLIRDS LISHGDRNIA SGALTDLIRL
     VETCGFHLHH LDVRQESTVH GEAVAQLLQQ LAPEVDYNTL DESDRQKVLS DLIAAPALAD
     LNREALDEGA LETLRVFEVI QAMRREIGPD GIGTYVISMT HAASHVLEVL LLGRLAGLAG
     EDESGEPFCH LRISPLFETI EDLLHVEDVL EGLLSNPVYA RLLTASGNVQ DVMLGYSDSC
     KDGGILASSW NLYEAQKKIV GITDRFGVRC QLFHGRGGTV GRGGGPTHES ILAQPPATVQ
     GRIKFTEQGE VLSYKYSNAE TAVYELGMGA TGLMLASRSL IRPARQDRDE YRATMDELAR
     AGEDAYRDLI DRTPGILDYF YEITPVQEIG FLNIGSRPSH RRKTDRSKSS IRAIPWVFGW
     AQSRHTLPAW YGIGSALEQW RGEDPARLEQ LQRMYQEWPF FRSLLSNCQM ALTKADMRTA
     AEYARLCSDP ALAERLYSRV REEHTRTVNE VLRVARLDNL MDETPLLARS LQRRNPYLDP
     LNSIQIHLLR ESRQFDAQAD DDADNPWLSP LLRSINAIAA GMRNTG
//
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