ID M0GX43_HALL2 Unreviewed; 897 AA.
AC M0GX43;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=C456_03866 {ECO:0000313|EMBL:ELZ76790.1};
OS Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)
OS (Haloferax alicantei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1230452 {ECO:0000313|EMBL:ELZ76790.1, ECO:0000313|Proteomes:UP000011535};
RN [1] {ECO:0000313|EMBL:ELZ76790.1, ECO:0000313|Proteomes:UP000011535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14919 / CCM 7023 / CIP 107410 / JCM 9276 / NCIMB 13854 / Aa
RC 2.2 {ECO:0000313|Proteomes:UP000011535};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(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}.
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:ELZ76790.1}.
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DR EMBL; AOLH01000006; ELZ76790.1; -; Genomic_DNA.
DR RefSeq; WP_004062362.1; NZ_AOLH01000006.1.
DR AlphaFoldDB; M0GX43; -.
DR GeneID; 80788252; -.
DR PATRIC; fig|1230452.3.peg.723; -.
DR Proteomes; UP000011535; Unassembled WGS sequence.
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:ELZ76790.1}.
SQ SEQUENCE 897 AA; 102453 MW; 8A03E8C396831BEE CRC64;
MRLHTRDVRQ DVRELGALLG DVLEAQTSTA SFETVEELRQ AAIAYRKGES GSRERLYDVV
GDLEPERESV VARAFTTYFE LINLAEERER VRVIREASQE GTLEDGILDT LDALDDEEVD
EELLGRVLED VLIEPTFTAH PTEARRKTVK SKLRSIANRL ETLDERRLTD LEHDQEWRHV
VAEVTSLWQT SQVRDRRPEP TDEARNVQWY LENTLFDVVG EVYEELEEEL RAEYPGLDVP
KLFEFRSWAG SDRDGNPFVT PEVTEDTLER QRSVALEKYS DALKRLSGVL SQDATRIDPG
HELERSLKAD REHLPVVAEE ADERYPNEPY RQKLKLMRER LRRVEDVRPN GYADASELMA
DLEVVDASLR RTGAEQVADV YVEPLMRQVD TFGFTLASLD LRDHQENHTE AVHEALAHEG
LDYYGSSEQE RVELLTDAIL QEEPVVDLED PGDVSETAER VLRRFRKLGE WQREYGVGAI
DTYCISMTEE PSHVLEVLFL ADQAGVVSLP DHCGIDVVPL LETESALNGA RRIMGTLFEN
EAYGTALAAR NDVQEIMLGY SDSNKENGFL AANWDLYKNQ RRLADICDDF DVTMRLFHGR
GGSISRGGGP MNEAMLALPN ETVTGQIKFT EQGEAIAEKY ANPRIAERNL EQMLNAQIRA
RLQAIRTPEE EVPDRWVDAM DTMAAAAREE YRDLLESDGF VSYFEQATPI TVIEELNLGS
RPASRSDERS VEDLRAIPWV FSWTQSRCIL PGWYSLAAGV NAFLEDGGDM DDLREMYDEW
AFFRSTFDNA AMALARTDLE IATEYANLAD EELREEFFTR LTEEYEDAAD LMLDISERSS
LLKREWLEES LRRRNPYVDP LNLLQTHLLS QTHRTDEEER TLRLTVKGIA AGMKNTG
//