ID A0A1K1TDW5_9GAMM Unreviewed; 882 AA.
AC A0A1K1TDW5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN ORFNames=SAMN02745752_00096 {ECO:0000313|EMBL:SFW98833.1};
OS Marinospirillum alkaliphilum DSM 21637.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinospirillum.
OX NCBI_TaxID=1122209 {ECO:0000313|EMBL:SFW98833.1, ECO:0000313|Proteomes:UP000182350};
RN [1] {ECO:0000313|EMBL:SFW98833.1, ECO:0000313|Proteomes:UP000182350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21637 {ECO:0000313|EMBL:SFW98833.1,
RC ECO:0000313|Proteomes:UP000182350};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC ECO:0000256|HAMAP-Rule:MF_00595}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00595};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR EMBL; FPJW01000001; SFW98833.1; -; Genomic_DNA.
DR RefSeq; WP_072324360.1; NZ_FPJW01000001.1.
DR AlphaFoldDB; A0A1K1TDW5; -.
DR STRING; 1122209.SAMN02745752_00096; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000182350; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
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; IPR033129; PEPCASE_His_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.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00595};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW Pyruvate {ECO:0000313|EMBL:SFW98833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182350}.
FT ACT_SITE 139
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 543
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 882 AA; 99070 MW; 06EB6739CD663D4C CRC64;
MTSLDTSLRE HVRILGESLG RTMSAAHGEE FLEQVESIRT LSKQVHQGEA TPQQLSESLR
QLDDEALLPV ARAFTQFLNL ANAAEQHYRA RERVVEDYRR GEQPGLTLLL NKLLEQGVAP
QRIAEALDAQ RVELVFTAHP TEVSRRTLIQ KYDALDACLA RYEQDSSEKN RAQVLRRLEE
IIAQAWHTDE IRSQRPSPVD EAKWGFAVIE NSLWQAVPAY YRALDEQLLR VCGQPLPLDA
APVRFASWMG GDRDGNPRVT ARVTQQVLWL SRWQAADLYH RDIDQLRAEL SMHQASEALV
QRVGPVREPY RVLLGQVRER LRATLDWLKA QLDGKPYDDE RILFDVDGLR EPLMLCYESL
CECGMQVIAD GLLRDILRRL SAFGMSLMRL DVRQEAPRHA QVLSEATRYL GLGDYAEWDE
QRRVDFLLHE LTNPRPLLPE SWPCSDESRE VLDTCRVIAA ERHDALGAYV ISMAGQPSDV
LAVALLLKTA GLERSMRIVP LFETLADLER APRVIDGLLS LPWYQTYTRG RQEVMIGYSD
SAKDAGQLAA SWAQYRAQEA VTEVCARHQV HLTLFHGRGG TVGRGGGPTQ AAILAQPPGS
VQGRLRVTEQ GEMIRFKFGL PALAERALEV YTCAVLEATL APPPAPRPEW RELMNRLAAD
AVASYRGMVR ETPDFVPYFR QLTPEQELAK LPLGSRPAKR KPGGGIESLR AIPWIFAWTQ
VRLMLPAWLG SDTALQQAVA RGETQALREM IEGWPFFASN INMLEMVLTK VDLASVVEYE
ELLVEDALKP LGAGLRDREQ QLVSCLLTLL QQQELLEQVP LTRQAISVRN PYIIPLHQLQ
AELLARVRAC EQQGVCSANP AMLERALMVT IAGIAAGLRN TG
//
