ID B9LS13_HALLT Unreviewed; 900 AA.
AC B9LS13;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN OrderedLocusNames=Hlac_2311 {ECO:0000313|EMBL:ACM57887.1};
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM57887.1, ECO:0000313|Proteomes:UP000000740};
RN [1] {ECO:0000313|EMBL:ACM57887.1, ECO:0000313|Proteomes:UP000000740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC {ECO:0000313|Proteomes:UP000000740};
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346}.
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DR EMBL; CP001365; ACM57887.1; -; Genomic_DNA.
DR RefSeq; WP_015911008.1; NC_012029.1.
DR AlphaFoldDB; B9LS13; -.
DR GeneID; 7401928; -.
DR KEGG; hla:Hlac_2311; -.
DR eggNOG; arCOG06225; Archaea.
DR HOGENOM; CLU_006557_2_0_2; -.
DR Proteomes; UP000000740; 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; 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.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACM57887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000740}.
FT COILED 636..667
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 900 AA; 102452 MW; 461A25A95092A05F CRC64;
MVLHNRDVRT DVRELGALVG DVLSAQTSTE AYETVEDLRH AAIDYRRGDA ASRDILRESV
EELSTTREEI VARAFTTYFE LINLAEERER VRAIRNADEN GSLHDSFDAT IAEFAEADVG
PDELRELLAD VLIEPTFTAH PTEARQATVK AKLRSIANHL EALDERNLTE RERNAIWRDI
TAEVTSLWST RQVRQRSPEP EDEARNVQWY LENTLFDVVG DAYEEFEETI SKEYDDVDCP
KLFEFRSWAG SDRDGNPFVT PEVTDETLAR QREVAVEKYR DRCKRLSAVL SQDGERYAVD
DRLAESLAAD VERFPTVVEE ARERYPDEPY RQKLRLMRER LDRVDDVRPG EYPDGDAFLA
DLDVIADSLA TDGQDAVRES FVEPLRRQVD TFGLTLASLD LRDHREKHTE TVAETVAVEG
VDYREMDEDA RQEFLTEAIL QDDPVVDADE PGDVSETTER VLRRFQEFAE WQDEYGPQAI
DTYCISMTEE PSHVLEVLFL ADQVGVVSLP DHCGLDVVPL LETESALNGA ERILGELFDN
EAYATALEVR GEIQEVMLGY SDSNKENGFL AANWDLYENQ RQIARFCREE DVTLRLFHGR
GGSISRGGGP MNEALLALPN ETVTGQVKFT EQGEAIAEKY ANRRIAEREL EQMLDAQIRA
RQEATEEPTE DVPDSWVDAM ETMAPAARET YRDLLNTDGF VSYFGQATPI SVVENLNLGS
RPASRSGERT VEDLRAIPWV FSWTQTRLIL PGWYSLASGI DAYLDEVGEE EGFETLQEMY
AEWPFFRTTL NNAALALART EPEIAAEYAD LADDDLRERF FPELIGEYER GRELVLEISG
RDELIRREWL AESLDRRNPY VDPLNLLQAN LLGRTHRTEE EERTLRLTVN GIAAGMKNTG
//
