ID A0A0U3H723_9MICC Unreviewed; 924 AA.
AC A0A0U3H723;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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:GEO91220.1};
GN ORFNames=AS188_01615 {ECO:0000313|EMBL:ALU38661.1}, KFL01_05260
GN {ECO:0000313|EMBL:GEO91220.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU38661.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU38661.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU38661.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO91220.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO91220.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) 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|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; CP013254; ALU38661.1; -; Genomic_DNA.
DR EMBL; BJZR01000008; GEO91220.1; -; Genomic_DNA.
DR RefSeq; WP_058857375.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U3H723; -.
DR STRING; 446860.AS188_01615; -.
DR KEGG; kfv:AS188_01615; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; 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; 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, 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:ALU38661.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000057181}.
FT ACT_SITE 145
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 585
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 924 AA; 100784 MW; D905AA6274D536BA CRC64;
MTEHDRPVPH RIDAPLRADV RRITTLLGET LVRQRGPELL ELVEQVRGLT KEAKASGDDD
AARRARELLG SLPLERATDL VRAFAHYFHL ANAAEQVHRV RLLGARPEAQ AWLAAAVADV
AGEAGPDGLR TAVERLDVRP VFTAHPTEAS RRSVLTKIRH LSDLLAEDTA EGTAARRRQD
RRLAELVELL WQTDELRRSR PTPLDEARNA LYYLREVLSG TVPGLLADLE DLLGEHEVAL
PAGPPLRFGS WIGGDRDGNP NVTPAITREV LRLQGQAAVD TALGFLELLV SRLSSSTAIV
AVEQELLDSV AEDVAHLPGL DARVLELNAQ EPYRLKLTCI KAKLLNTRRR FAEETAHEPG
RDYRSTGQLL ADLDVVARSL RAHAGERAAG GALAAAARTI AGSGLVLASL DVREHADAHH
EAVGQLLDRL GEHDRPYAQL DRAGRTRVLA AELAGRRPLA PPGLATGTVQ LEGDADRTFA
VFREIGRAQA VYGEEAVETY IVSMTRGADD ILAPVVLARE AGLVDLTGER PRAGLGFAPL
LETVHELRRS AEVIDELLSD PAYREVVRAR GDLQEVMLGY SDSNKESGVM TSRWEIHRTE
RRLRDVAARH GVRLRLFHGR GGSVGRGGGP THDAILAQPG GVLDGEIRFT EQGEVISDKY
SLPALARENL ELSLAAVLRA TALHQGPRSS EAELERWGQV MDVVSDAAFA AYRGLIEDPD
LPEYFVTATP VEQLGALNIG SRPSKRPSSD AGIEGLRAIP WVFGWTQSRQ IVPGWFGVGS
GLRAAREAGM AQDLAAMLER WHFFASLVSN VEMTVAKTDL GIAAQYVSAL VPERLHHVFD
TVRAEFALTC EELARLTGQA EPLDDNPVLQ QTLAVRDQYL DPISHLQVEL LRRLREAGGE
PDEQLQRAML ITINGIAAGL RNTG
//
