ID   D2S1E1_HALTV            Unreviewed;       896 AA.
AC   D2S1E1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   OrderedLocusNames=Htur_4375 {ECO:0000313|EMBL:ADB63188.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG   Plasmid pHTUR01 {ECO:0000313|EMBL:ADB63188.1,
OG   ECO:0000313|Proteomes:UP000001903}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63188.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB63188.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RC   PLASMID=pHTUR01 {ECO:0000313|EMBL:ADB63188.1,
RC   ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; CP001861; ADB63188.1; -; Genomic_DNA.
DR   RefSeq; WP_012945432.1; NC_013744.1.
DR   AlphaFoldDB; D2S1E1; -.
DR   GeneID; 8745003; -.
DR   KEGG; htu:Htur_4375; -.
DR   HOGENOM; CLU_006557_2_0_2; -.
DR   OrthoDB; 340936at2157; -.
DR   Proteomes; UP000001903; Plasmid pHTUR01.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ADB63188.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Plasmid {ECO:0000313|EMBL:ADB63188.1};
KW   Pyruvate {ECO:0000313|EMBL:ADB63188.1}.
SQ   SEQUENCE   896 AA;  101866 MW;  3B6B9BA5BEB3E903 CRC64;
     MELHDRSISQ DIHDLGALLG NILEEQTSLE AFETVKSCRR AAIDYRSGDL DTRDPLIAEL
     EGLSPHNQRI VARAFTTYFE LINLAEERER IRTIRTGSHE RTLDDGLEDA AAELGEADDE
     TVQRILDDIL IEPTFTAHPT EARRKTVKSK LRDISTSLET LDERLLTEKE EEQVWRDIDA
     EVTSLWQTPQ VRNRQPEPED EARNVQWYLE NTLFDVVGEV YDELDDAIDS ELPRDIDVPK
     LFEFRSWAGS DRDGNPYVTP EVTANVLERQ REVVLEKYRD ELKRLSGVLS QDGGRIDAGG
     EFEASLEVDR ERLPSVARTA EERYPGEPYR QKLKLMRERL RRVGDVRPGG YDDVDELLED
     LDVIATSLRN NGGETVVEAH VDPIRRRVDT FGFSLASLDL RDHQQKHTDA IAEALEREGI
     DYRGLSEAER VEFLTDAVLQ DEPVLDLGET DGLTDDSTRV LELFDSLADW QTEYGVEAID
     TYCISMTDEP SHVLEVLFLA DQAGVVSLPE HSGIDIVPLL ETEYALSGAR RIMGTLFENE
     AYSQALEARG RTQEIMLGYS DSNKENGFLA ANWSLHKNQR RLGEICDDHD VTMRLFHGRG
     GSISRGGGPM NEALLALPNN TITGQVKFTE QGEAIAEKYG NPRIAERNIE QMLNAQLRAR
     KQAIDQPEED VHAEWIDAME TMADAARQEY RDLLESDGFV RYFEQATPIT VIEDLNLGSR
     PASRSGERTV EDLRAIPWVF SWTQSRCILP GWYALATGIE AYLDNGGSMD TLQEMYDEWP
     FFRTTLDNAA LSLSRTELEI AEQYAGMADA ALRDRFFPRV TDEYERATEL ITEIGQRDRL
     HTRDWLGENL EQRNPYVDPL NMLQVHLLDR NHRTNIEERT LRLTVKGIAA GMKNTG
//