ID A0A1M5MGH6_9EURY Unreviewed; 900 AA.
AC A0A1M5MGH6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=SAMN05443636_1007 {ECO:0000313|EMBL:SHG76420.1};
OS Halobaculum gomorrense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halobaculum.
OX NCBI_TaxID=43928 {ECO:0000313|EMBL:SHG76420.1, ECO:0000313|Proteomes:UP000184357};
RN [1] {ECO:0000313|EMBL:SHG76420.1, ECO:0000313|Proteomes:UP000184357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9297 {ECO:0000313|EMBL:SHG76420.1,
RC ECO:0000313|Proteomes:UP000184357};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQWV01000002; SHG76420.1; -; Genomic_DNA.
DR RefSeq; WP_073307300.1; NZ_FQWV01000002.1.
DR AlphaFoldDB; A0A1M5MGH6; -.
DR STRING; 43928.SAMN05443636_1007; -.
DR OrthoDB; 340936at2157; -.
DR Proteomes; UP000184357; 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:SHG76420.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184357}.
SQ SEQUENCE 900 AA; 99932 MW; 04BEF3E44B4BA768 CRC64;
MSFDARDVGR DIRELAALLG EVLERQTSTD AFDTVEEVRR ASIDYRRGDA PSRDPVRDRL
SGLDSETTRT VARAYAAYFE LVNVAEERER VRAVRRGRAE GDLGDGLDRT AEALAAVDAE
TAQQVLEDVR VVPTFTAHPT EARRKTVKAK LRRVAEILRD LDERRLTDGE LDELDRDLES
EVETLWSTRQ VRPRRPTPTD EARDVRWYLE NTLFDVAAEA EAALTDRVVE AHPDLDASDA
ADAAGTLDFR SWAGSDRDGN PFVTPEVTSD TLEAQREAVL DRYVDALTDV RGALSHEGER
LDHTDEFEAR VAADREAVPA VAADADERYP EEPYRRAATA VRARVERVDD LRPGGYDDPD
DLVASLRALA ADLRANGHET TAAERVDPLV RRVETFGFSL AALDLRDHQE NHTETVADVL
AREGLDYEAM DEGERVAVLT ESVVDDSIGS LDSGEGLSET SERVCRRFRA LADWHREYGE
EAIDAYCISM TEEPSHVLEV LYLADLAGVV DLPDHCGLDV VPLLETASAL ANARDILGTL
VNNDAYGAAL SARGDVQEVM LGYSDSNKEN GPLAAAWDLH QNARRLAEVA DDLGVELRLF
HGRGGSISRG GGPMNEAMLA LPPETATGEI KFTEQGEAIA EKFANPRVAE RELEQMLDAQ
VRARLRALQG NAQEVHDEWE AAMDAAGEGA RAAYQDLLET DGFVEFFETA TPITVIEDLN
MGSRPASRSG ERTVEDLRAI PWVFSWTQSR AILPGWFSSA SGLDAYLSDG GDLDTLREMY
EEWPFFRTTI DHIALSLART ELEIAAEYAD LAPEHLREEF FARIEAEYER AVELVREITG
HDELVRREWL AESLQRRNPY VDPLNLLQVD LLSRTHLTEA EERALRLTVK GIAAGMKNTG
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