ID A0A0E9MMQ6_9SPHN Unreviewed; 888 AA.
AC A0A0E9MMQ6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ECO:0000313|EMBL:GAO38706.1};
GN ORFNames=SCH01S_19_00100 {ECO:0000313|EMBL:GAO38706.1};
OS Sphingomonas changbaiensis NBRC 104936.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO38706.1, ECO:0000313|Proteomes:UP000033202};
RN [1] {ECO:0000313|EMBL:GAO38706.1, ECO:0000313|Proteomes:UP000033202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO38706.1,
RC ECO:0000313|Proteomes:UP000033202};
RA Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL Submitted (APR-2015) 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:GAO38706.1}.
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; BBWU01000019; GAO38706.1; -; Genomic_DNA.
DR RefSeq; WP_046347557.1; NZ_BBWU01000019.1.
DR AlphaFoldDB; A0A0E9MMQ6; -.
DR STRING; 1219043.SCH01S_19_00100; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000033202; 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:GAO38706.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033202}.
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 555
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 888 AA; 96479 MW; 31DE9C4F7281B7E6 CRC64;
MSEAHTISQN PDIRFLGRML GNVIRHYGGE TLYRRTEYIR SASVDRARGL ADAESIDPGL
DALSLDDTLA FVRGFMLFSM LANLAEDRQG VAAEPGADVA HAVERLRGEG IGDEAIAALL
KDALIAPVLT AHPTEVRRKS VIDHRNRIAE LMQLRDTGAV ETPEGEPVEL AIERQIALLW
QTRPLRRERL YVADEVETAR TYFQDVFLPV LPALYARWER ALGERPPSFV RPGSWIGGDR
DGNPFVTADS LRLALSRGAE TAIAHYLDCL HALGAELSVS SGLADVEPAV IALAEASHDE
AAARIDEPYR RAISGIYARL SASFEALTGH APPRPTRIVA DPYSSPEALA ADLRVLGRSI
GGAGGPLAGP GPLGRLIRAV ETFGFHMATL DLRQNSAVHE RVVGELLARA GVEAVYAALD
EAGRVALLLR ELGSARLLSS PFADYSDETR SELEIARAAA EAHARYGPAS IRAYIVSMCK
SVSDLLEVHI LLKEAGLFVP GKPPAIMAVP LFETIADLEA APFIMRDWFG LPGIVEWARE
RGRQEVMLGY SDSNKDGGYL TSVWSLYRAS EALRDIFAEA SVAMQLFHGR GGAVGRGGGS
SFAAIRGQPT GTVQGCIRIT EQGEVIAAKY GTPESAATNL EAITAATLLA SLEPPSLSGS
DKARFEDAMA ELSRTAFQDY RGLVYETDGF RSFFRQMTPI AEIATLKIGS RPASRTKSDA
IEDLRAIPWV FSWAQARVML PGWYGVGHAL AAFGDKALLR EMAEAWPFFA PTLGNLEMVL
AKSDMGIAAR YAGLVEDRQT ADAIFGRIRD GWYRTRDILL EVTDQSRLLE KTPGLDTSIR
LRMPYVEPLN LLQIELLKRH RAGEADPRIA EGIQLSINAI ATALRNSG
//
