ID   D2RVU2_HALTV            Unreviewed;       897 AA.
AC   D2RVU2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   OrderedLocusNames=Htur_2494 {ECO:0000313|EMBL:ADB61371.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB61371.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB61371.1, 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};
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; CP001860; ADB61371.1; -; Genomic_DNA.
DR   RefSeq; WP_012943651.1; NC_013743.1.
DR   AlphaFoldDB; D2RVU2; -.
DR   STRING; 543526.Htur_2494; -.
DR   GeneID; 8743104; -.
DR   KEGG; htu:Htur_2494; -.
DR   eggNOG; arCOG06225; Archaea.
DR   HOGENOM; CLU_006557_2_0_2; -.
DR   OrthoDB; 340936at2157; -.
DR   Proteomes; UP000001903; Chromosome.
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:ADB61371.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:ADB61371.1}.
FT   REGION          296..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   897 AA;  102006 MW;  E7A1909E51EC8456 CRC64;
     MRLHNREIRQ DVRELGALLG DVLEDQTSRQ GFETVESCRR AAIDYRSGDL ESREPLISRL
     EGLSPHNQRI VARAFTTYFE LINLAEERER VRTIRTESNE GTLEDSLEMA AEELGERGVD
     TVEDVLDDVL IEPTFTAHPT EARRKTVKSK LRTISTHLET LDERLLTEKE QSQVWRDIDA
     EVTSLWQTPQ VRNRQPEPED EARNVQWYLE NTLFDVVGEV YDELADAIDA ETAGDLEIPK
     LFEFRSWAGS DRDGNPYVTP EVTANVLERQ REVVLEKYRD ELKRLSGVLS QDGSRIDTGG
     EFEASLEDDR ERLPGSARTA EDRYPGEPYR QKLKLMRERL ARVGDVRPGG YDDVDELLDD
     LAVIAQSLRN NSGESVVEAH VDPIRRQVAT FGFSLASLDL REHQQKHTGA IAEALEREGI
     DYRSLSEDER VELLTDAVLQ DDPLVDLSET SDLSEDSARV LELFDSLGDW QTEYGVEAID
     TYAISMTDEP SHVLEVLFLA DQAGVVSLPE HAGIDIVPLL ETEYALSGAR RIMGTLFENE
     AYSQALEARG RTQEIMLGYS DSNKENGFLA ANWSLFKNQR RLGEICDDYD VQMRLFHGRG
     GSISRGGGPM NEALLALPNN TITGQVKFTE QGEAIAEKYA NPRIAERNIE QMLNAQLRAR
     LYAKEEPDEE ELPEEWFDAM ETMADAARQE YRDLLESDGF VQYFEQATPI SVIEDLDLGS
     RPASRSGERT VEDLRAIPWV FSWTQSRCIL PGWYAVAAGI DAYLEDGGSM ETMQEMYDQW
     PFFRTTLDNA ALSLSRTELE IADQYADLAD SELRERFFPR ITDEYQRATE LITEIGQRED
     LHTRDWLGEN LARRNPYVDP LNVLQVYLLD RNHRTDVEER TLRLTVKGIA AGMKNTG
//