ID A0A0C2JJJ4_9ACTN Unreviewed; 852 AA.
AC A0A0C2JJJ4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=LP52_21610 {ECO:0000313|EMBL:KIH97072.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH97072.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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}.
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:KIH97072.1}.
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DR EMBL; JROO01000044; KIH97072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2JJJ4; -.
DR STRING; 183763.LP52_21610; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000031675; 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; 2.
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:KIH97072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031675}.
FT ACT_SITE 122
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 852 AA; 94469 MW; AF62B35E3BCF59B9 CRC64;
MLGTVMAESG GEDLLSDVER LRRAVIGARD GSVSGEEITE LVDSWPLERA KQVARAFTVY
FHLANLAEEH QRIRALRERD DADNPPRESL AAAVHAIRES AGEETLRELV ENMEFHPVLT
AHPTEARRRA VSTAILRISG QLDRLHGAHP GSTAEAETKR RLLEEIDLLW RTSQLRYTKL
DPLDEVRTAL AAFDETIFQV VPEIYRALDA AIDPDGTGRE PVRARPFVRY GSWIGGDRDG
NPFVTHDVTR EAISIQAEHV LRALENACGR VARTLTVYSN LTPAGQELRD ALAAAEAGYP
RIMAEITKRS PNEPHRQALL FATERLRATR ERNADLAYRG PEEFLTELRR VQDSLARAGA
ARQANGELQH LIWQAETFGF HLAELEIRQH SEVHAQALEE LRAGGQVSER TQEVLATLRV
VAWIQERFGV DACRRYIVSF TRSADDIAAV YELAEYAMPT GQTPVLDVIP LFETGADLEA
SPHVLDGMLR LPRMRARLEE TGRRMEVMLG YSDSAKDVGP VSATLRLYDA QAHLASWAER
NDVRLTMFHG RGGSLGRGGG PANRALLAQA PGSVAGRFKV TEQGEVIFAR YGQRAIAHRH
IEQVGHAVLM ASTEEVQERA NAAASKYRTL ADGISRAAHD AYRSLIETEG FAEWFSAVSP
LEELGELRLG SRPSRRSAAR GLDDLRAIPW VFAWTQTRVN LPGWFGLGTG LAAAPDLSEL
QAAYNEWPLF SSLLDNAEMS LAKTDRAIAE RYLALGGRPE LTRVVLDEFD RTSDLVLKVT
GHERLLENRS VLSRAVDLRN PYVDALSHLQ LRALSALRGA EEESLSEEDE RHLERLLLLT
VNGVAAGLQN TG
//
