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Database: UniProt/TrEMBL
Entry: V5TLY9_HALHI
LinkDB: V5TLY9_HALHI
Original site: V5TLY9_HALHI 
ID   V5TLY9_HALHI            Unreviewed;       898 AA.
AC   V5TLY9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=HISP_06475 {ECO:0000313|EMBL:AHB65670.1};
OS   Haloarcula hispanica N601.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=1417673 {ECO:0000313|Proteomes:UP000018572};
RN   [1] {ECO:0000313|EMBL:AHB65670.1, ECO:0000313|Proteomes:UP000018572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N601 {ECO:0000313|EMBL:AHB65670.1,
RC   ECO:0000313|Proteomes:UP000018572};
RX   PubMed=24625874;
RA   Ding J.Y., Chiang P.W., Hong M.J., Dyall-Smith M., Tang S.L.;
RT   "Complete Genome Sequence of the Extremely Halophilic Archaeon Haloarcula
RT   hispanica Strain N601.";
RL   Genome Announc. 2:e00178-14(2014).
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; CP006884; AHB65670.1; -; Genomic_DNA.
DR   RefSeq; WP_014040139.1; NC_023013.1.
DR   AlphaFoldDB; V5TLY9; -.
DR   GeneID; 23805340; -.
DR   KEGG; hhn:HISP_06475; -.
DR   HOGENOM; CLU_006557_2_0_2; -.
DR   Proteomes; UP000018572; Chromosome 1.
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};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:AHB65670.1}.
SQ   SEQUENCE   898 AA;  103132 MW;  E8ACE5BC4D363C6B CRC64;
     MTLHAREINQ DVRELGALLG EVLEAQTSTE AFETVETIRT SCIDYRRGDA ETRDEVHRAL
     NRLNPETQDI VARAFTTYFE LINLAEERER VREIREGSEE GVLADSVEEA VRDLAERGAD
     PEEFEQVLED VLIQPTFTAH PTEARRKTVK AKLRSVARDI ERLDERRLTE REQKRIERNL
     DAEVTSLWQT PQVRDRRPEV TDEALNVQWY LENVLFDVID EVYDELEHTL EDVYDEDIDI
     DTLYEFRSWA GSDRDGNPFV TTEVTEETLE RQRDTVLPLY RNKLKELSGV LSQDASNIAT
     DALFNERLDR HKSRLPGIAT EAEERYPDEP YRQKLRLMRE SVIRVSDVRQ GGYESDEELL
     TDLRVIADSL RENDAEVIAE AHVDPLIRKV ETFGFNLASL DLRDHRKMHT DAIAESVERE
     GIDYAGMDED ERVEFLTEAI IQDNPVIDME DTEGLSEDAT RVLDRFRAAA DWQNEFGIDA
     IDTYAISWCE EPSHALEVLF LADQVDIVDL PGYCGFDVVP LLESEYALSG ARRIMGTLFE
     NEAYSQALEA RDNIQEIMLG YSDSNKENGF LAANWSLYNN QKRLADITDD YDVEMRLFHG
     RGGSISRGGG PMNDAMLALP NETVTGQIKF TEQGEAIAEK YANHDIAERN LEQMLNAQIR
     ARKNAIEEPV EEIPDEWEEA METASDAARN EYQDLLETDG FVEFFEQATP ITVIENLNMG
     SRPASRSEDR SVEDLRAIPW VFSWTQARCI IPGWYSIATG LDAYLENGGD METLQEMYEN
     WPFFRTKLDN ASLALARTDL EIAEEYADLA DPELRERIYP RIVEEYEDTV EKVLEITGQD
     GLLSREWLQE NLERRNPYVD PLNLLQVRLL KQSHRTDTER RTLRLTVQGI AAGMKNTG
//
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