ID A0A197STG3_9ACTN Unreviewed; 909 AA.
AC A0A197STG3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=A8W25_11915 {ECO:0000313|EMBL:OAR26154.1};
OS Streptomyces sp. ERV7.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1322334 {ECO:0000313|EMBL:OAR26154.1, ECO:0000313|Proteomes:UP000078470};
RN [1] {ECO:0000313|EMBL:OAR26154.1, ECO:0000313|Proteomes:UP000078470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERV7 {ECO:0000313|EMBL:OAR26154.1,
RC ECO:0000313|Proteomes:UP000078470};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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}.
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:OAR26154.1}.
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DR EMBL; LYOY01000029; OAR26154.1; -; Genomic_DNA.
DR RefSeq; WP_067159973.1; NZ_LYOY01000029.1.
DR AlphaFoldDB; A0A197STG3; -.
DR STRING; 1322334.A8W25_11915; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000078470; 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:OAR26154.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078470}.
FT ACT_SITE 135
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 567
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 909 AA; 100639 MW; E724C5E60FB8BA31 CRC64;
MSSADQTPAA SPELRADIRR LGDLLGEALV RQEGPELLEL VERVRALTRT DGEAAAELLG
GTEVETAAKL VRAFSTYFHL ANVTEQVHRG RELRAHRAAE GGLLARTADM LKDADPEHLR
ETVKNLNVRP VFTAHPTEAA RRSVLNKLRR IAALLETPVT EADRRRHDLR LAENIDLIWQ
TDELRVVRPE PADEARNAIY YLDELHANAV GDVLEDLAAE LERVGVELPP GTRPLTFGTW
IGGDRDGNPN VTPQVTWDVL ILQHEHGIND ALEVIDFLRG LLSNSIRYAG ATEELLASLQ
ADLEALPEIS PRYKRLNAEE PYRLKATCVR QKLVNTKERL AKGTPHLPGR DYLGTSELLA
DLTLIQTSLR AHRGALFADG RMDRTIRTLA AFGLQLATMD VREHADAHHH ALGQLFDRLG
EESWRYADMP REYRQKLLAK ELRSRRPLAP TPAPLDEAGQ KTLGVFGTIK EAFERFGPEV
IESYIISMCQ GADDVFAAAV LAREAGLVDL HAGWAKIGIV PLLETTDELR AADVILDEML
ADPSYRRLVS LRGDVQEVML GYSDSSKFGG ITTSQWEIHR AQRRLRDVAH RYGVRLRLFH
GRGGTVGRGG GPSHDAILAQ PWGTLEGEIK VTEQGEVISD KYLIPSLARE NLELTVAATL
QASALHTAPR QSDEALARWD AAMDTVSDAA HSAYRKLVED PDLPAYFFAS TPVDQLAELH
LGSRPSRRPD SGAGLDGLRA IPWVFGWTQS RQIVPGWFGV GSGLKALREA GLDTVLDEMH
EQWHFFQNFI SNVEMTLAKT DLRIARHYVD TLVPDELKHV FADIEAEHAL TVSEVLRITG
GEELLGSHPV LQQTFAIRDA YLDPISYLQV SLLARQRAEA ERGENPDPLL ARALLLTVNG
VAAGLRNTG
//
