ID A0A063ZS70_9EURY Unreviewed; 896 AA.
AC A0A063ZS70;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=EL22_18645 {ECO:0000313|EMBL:KDE59706.1};
OS Halostagnicola sp. A56.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=1495067 {ECO:0000313|EMBL:KDE59706.1, ECO:0000313|Proteomes:UP000027027};
RN [1] {ECO:0000313|EMBL:KDE59706.1, ECO:0000313|Proteomes:UP000027027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A56 {ECO:0000313|EMBL:KDE59706.1,
RC ECO:0000313|Proteomes:UP000027027};
RA Pore S.D., Kanekar S.P., Arora P., Saxena N., Dhakephalkar P.K.;
RT "Draft genome of Halostagnicola sp. A56 isolated from Andaman Islands,
RT India.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KDE59706.1}.
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DR EMBL; JMIP02000014; KDE59706.1; -; Genomic_DNA.
DR RefSeq; WP_050050452.1; NZ_JMIP02000014.1.
DR AlphaFoldDB; A0A063ZS70; -.
DR STRING; 1495067.EL22_18645; -.
DR OrthoDB; 340936at2157; -.
DR Proteomes; UP000027027; 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:KDE59706.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027027}.
FT REGION 301..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 101768 MW; 311B71AF1DD35505 CRC64;
MDLHNRDVRQ DVRELGALLG DVLEQQTSRR AFDTVESCRQ TAIEYRSGDL ESRDPLISEL
EGLSPHQQRI VARAFTTYFE LINLAEERER VRSIRQGSQE GSLADSLEMV AEELGEEDLE
TAQQILDDVL IEPTFTAHPT EARRKTVKSK LRAVANHLET LDERLLTDKE RSQVWRDVDA
EVTSLWQTPQ VRKRQPEPED EARNVQWYLE NTLFDVVGEV YDEFGVALED ELEGDVDLPK
LFEFRSWAGS DRDGNPYVTP EVTANTLERQ RSVVLERYRE QLKRLSGVLS QDGSRLEVDG
PFEASLETDR ERLPGSAQTA ETRYPGEPYR QKLKLMRERL DRVGDVRPGG YPDADELLGD
LELIATSLRE NGAETVVEAH VDPILRQVET FGFSLASLDL REHQAKHTDA IAEALEREGI
DYRGLSEDER VEFLTDAVLQ DETVIDLEAV EDLSDASARV LTLFDELADW QTEYGVEAID
TYAISMTDEP SHVLEVLFLA DQSGIVSLPE HCGIDIVPLL ETEYALSGAR RIMGTLFENE
AYAKALEARG RTQEIMLGYS DSNKENGFLA ANWSLYKNQR RLGEICDDYD VTMRLFHGRG
GSISRGGGPM NEALLALPNS TVTGQVKFTE QGEAIAEKYG NPRIAERNIE QMLNAQLRAR
RNAINQPEEE IREEWFEAME TMATAARQEY RDLLESDGFV QYFEQATPIT VIEDLDLGSR
PASRSSERTV EDLRAIPWVF SWTQSRCILP GWYAIAAGVS AYLDDGGSIE TLQEMYDEWA
FFRSAFDNAA LSLSRTELEI AAEYADLAED DLREEFFSRL TDEYEQAAEY VTTIGRRDQL
HTRDWLGENL ERRNPYVDPL NVLQTYLLDQ SHRTDVEERT LRLTVKGIAA GMKNTG
//