ID G5J8N4_CROWT Unreviewed; 1016 AA.
AC G5J8N4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=CWATWH0003_3812 {ECO:0000313|EMBL:EHJ11452.1};
OS Crocosphaera watsonii WH 0003.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ11452.1, ECO:0000313|Proteomes:UP000003477};
RN [1] {ECO:0000313|EMBL:EHJ11452.1, ECO:0000313|Proteomes:UP000003477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ11452.1,
RC ECO:0000313|Proteomes:UP000003477};
RX PubMed=22232617;
RA Bench S.R., Ilikchyan I.N., Tripp H.J., Zehr J.P.;
RT "Two Strains of Crocosphaera watsonii with Highly Conserved Genomes are
RT Distinguished by Strain-Specific Features.";
RL Front. Microbiol. 2:261-261(2011).
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:EHJ11452.1}.
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DR EMBL; AESD01000570; EHJ11452.1; -; Genomic_DNA.
DR RefSeq; WP_007311794.1; NZ_AESD01000570.1.
DR AlphaFoldDB; G5J8N4; -.
DR PATRIC; fig|423471.3.peg.3577; -.
DR Proteomes; UP000003477; 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:EHJ11452.1}.
FT REGION 110..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 663
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1016 AA; 116713 MW; 9E1FAE48556519E7 CRC64;
MLLESLQSTV EEVNIFSTSD LFLRQRLELV ESLWESVLKA ECGLELVDLL KKLRKISSPE
GQVTHQPKTS INELIEELEL NEAIRATRAF ALYFQLINIV EQHYEQRDQQ LNRRSTYQES
EKARENYQKG EKSTNGLVGA DLLEKALVGE TKSQEKGGTF HWLFPQLKRL NVPPQQIQRL
LEQLDIRLVF TAHPTEIVRH TIRLKQRRIA TLLRRLDQAE EAFRGMGLSS SWEAESIIEQ
LNEEIRLWWR TDELHQFKPS VLDEVDYTLH YFDEVLCSAL PQLSQRLQQA LQANFPRIKP
PHNTFCRFGS WVGGDRDGNP FVTTDVTWRT ACYQRNLILE KYLAAVEDLT EILSSSLHWS
NVSQDLLDSL ERDRVAMPEI YDQLAIRYRQ EPYRLKLAYI QKRLEHTRDR NNHLANPEQG
QVLVEETPEN IYHSGVEFEA ELQLIKRNLE ETGLKCQALE NLIFQAQMFG FTLTQLDFRQ
ESSRHSETIQ TIASYLNILP TPYEELSEAE KVNWLVGELQ TRRPLIPMEM PFDEKTIETV
ETMRMLRHLQ QEFGIEICQT YIISMTNDVS DVLEVLLLAK EAGLYDPGTS TTTIRIVPLF
ETVDDLKRAP EIMEALFKLP LYRAALAGGY DYLDEDKKEQ LPPPQLQPAN LQEIMVGYSD
SNKDSGFLSS NWEIHKAQKS LQKIAEPHNL ALRLFHGRGG SVGRGGGPAY AAILAQPTGT
INGRIKITEQ GEVLASKYSL PELALYNLET ATTAVIQGSL LGSGFDDIDP WNGIMEELAS
SARKAYRSLI YEQPDFLDFF LSVTPIPEIS QLQISSRPAR RKSGKKDLST LRAIPWVFSW
TQSRFLLPAW YGVGTALEGF LQQEPEENLK LFKYFYLKWP FFKMVISKVE MTLSKVDLQI
AHHYVKELSD PEDIERFEKV FERISEEYHR TCEIILSITG QPKLLEGDAG LQRSVQLRNG
TIVPLGFLQV SLLKRLRQYT RQAESGVIHF RYSKEELLRG ALLTINGIAA GMRNTG
//
