ID A0A0L6CN30_9MICO Unreviewed; 922 AA.
AC A0A0L6CN30;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=VV01_04605 {ECO:0000313|EMBL:KNX39196.1};
OS Luteipulveratus halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=1631356 {ECO:0000313|EMBL:KNX39196.1, ECO:0000313|Proteomes:UP000037397};
RN [1] {ECO:0000313|Proteomes:UP000037397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C296001 {ECO:0000313|Proteomes:UP000037397};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-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:KNX39196.1}.
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DR EMBL; LAIR01000002; KNX39196.1; -; Genomic_DNA.
DR RefSeq; WP_050671720.1; NZ_LAIR01000002.1.
DR AlphaFoldDB; A0A0L6CN30; -.
DR STRING; 1631356.VV01_04605; -.
DR PATRIC; fig|1631356.3.peg.863; -.
DR Proteomes; UP000037397; 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:KNX39196.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037397}.
FT ACT_SITE 153
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 584
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 922 AA; 101782 MW; 5923C8D655CBC4B6 CRC64;
MSAHLVFDVS AEGRAATEPL REDIRLLGGM LGDVVREQEG ERVFELVEDA RRRAFAVRRE
EVDREGFADL FRDLPTTDAL HVIRAFSLFA LLANLAEDLH RERRRALHVR AGDPAPDGSL
AASFAKLAAA GLDPAEVADA LTDATVVPVI TAHPTETRRR TVFEAQTRIK ETMRTRERMA
LTDVEEADAL RAIKIQVITL WQTALIRLQR VQIQDEIEVG LRFFEASLFE VMPQINARLR
SELGELFPDA DLAAEPVLRA GSWIGGDRDG NPNVNADVVA TASSRASQTA IQHYLTELTE
LETALSLSVR MTDVTDDLRA LAALNTTDER DDEPYRRALA WARGRLAATY VQFFGQPARR
AYDVAGATAY DTPDALLADL DVIDASLRGD GDDLLADDRL LRLREAVRTF GFHLYGLDLR
QNSDVHEETV AELFAWAGVH DAYADLDEDA KVALLVDELQ SRRPLIGGAA DLSEQTTREL
AITAAAAHAV RTFGAGAVPN YVISMCTSVS DLLECAVLLK EAGLLDPVAG TCPVNVVPLF
ETIEDLQVSA TTLRAALAVP VYRALVDSKG RLQEVMLGYS DSNKDGGYLA ANWALYRAEL
DLVEVAREHD IRLRLFHGRG GTVGRGGGPS YEAILAQPPG AVRGSLRLTE QGEIIAAKYA
EPRLATRNLE ALVSATLEAS LLDTERLGEQ SDAAYEHLDD LAALAREAYA DLVHRTDGFV
EYFKTSTPVA EIGALNIGSR PASRKPTEQI SDLRAIPWVM SWSLSRVMLP GWYGTGSALE
QWVGGDADRL KTLRGYYERW PFFQTVISNL AQVMAKSDLG IAERYSRLVP DEALRERVFG
KIVDEHERTV RMVQEVTGRD DLLWDNAALK RSVFNRFPYL EPLNHLQVEL LHRYRSGDES
EQLRRGILLT MNGLATALRN SG
//
