ID A0A1S2KAS3_9ACTN Unreviewed; 909 AA.
AC A0A1S2KAS3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BJP40_17575 {ECO:0000313|EMBL:OII65196.1};
OS Streptomyces sp. CC53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII65196.1, ECO:0000313|Proteomes:UP000179639};
RN [1] {ECO:0000313|EMBL:OII65196.1, ECO:0000313|Proteomes:UP000179639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC53 {ECO:0000313|EMBL:OII65196.1,
RC ECO:0000313|Proteomes:UP000179639};
RA Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT transport.";
RL Submitted (OCT-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:OII65196.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKXB01000055; OII65196.1; -; Genomic_DNA.
DR RefSeq; WP_071278852.1; NZ_MKXB01000055.1.
DR AlphaFoldDB; A0A1S2KAS3; -.
DR STRING; 1906740.BJP40_17575; -.
DR Proteomes; UP000179639; 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:OII65196.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179639}.
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; 101044 MW; 49ADDC312684C003 CRC64;
MSSADQTPSA STELRADIRR LGDLLGETLV RQEGPELLEL VEKVRRLTRE DGDAAAELLR
GTELETAAKL VRAFSTYFHL ANVTEQVHRG REMRARRAAE GGLLARTADM LKDGDPQHVR
ETVKHLNVRP VFTAHPTEAA RRSVLNKLRR IAALLDEPVT AADRRRHDLR LAENIDLIWQ
TDELRVVRPE PADEARNAIY YLDELHAGAV GDVLEDLAAE LERVGVELPP GTRPLTFGTW
IGGDRDGNPN VTPAVTWEVL ILQHEHGLND AIDMIDELRG LLSNSIRYAG ATQELLDSLQ
KDLDRLPEIS PRYKRLNAEE PYRLKATCIR QKLENTRDRL AKGTPHQEGR DYLGTAELLH
DLGLIQTSLR EHRGGLFSEG HLDRTIRTLS AFGLQLATMD VREHADAHHH TLGQLFDRLG
EESWRYADMP REYRQKLLAK ELRSRRPLAP SPAPLDAAGQ KTLGVFHTVK AAFERFGPEV
IESYIISMCQ GADDVFAAAV LAREAGLVDL HAGWAKIGIV PLLETTDELR AADVILNDML
ADPSYRRLVA LRGDVQEVML GYSDSSKFGG ITTSQWEIHR AQRRLRDVAH RYGVRLRLFH
GRGGTVGRGG GPSHDAILAQ PWGTLEGEIK VTEQGEVISD KYLIPSLARE NLELTVAATL
QASALHTGPR QTHEALARWD AAMDTASEAA HTAYRSLVED PDLPAYFFAS TPVDQLAELH
LGSRPSRRPD SGAGLDGLRA IPWVFGWTQS RQIVPGWFGV GSGLKALRDA GLDDVLGEMY
EKWHFFRNFL SNVEMTLAKT DLRIARHYVE TLVPEHLRHV FATIEAEHAL TVEQVLRVTG
EKELLDAQPV LKQTFAIRDA YLDPISYLQV ALLKRQRDAA AAEAPADPLL ARALLLTVNG
VAAGLRNTG
//
