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Database: UniProt
Entry: D6AJ68_STRFL
LinkDB: D6AJ68_STRFL
Original site: D6AJ68_STRFL 
ID   D6AJ68_STRFL            Unreviewed;       909 AA.
AC   D6AJ68;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=SSGG_02533 {ECO:0000313|EMBL:EFE75166.2};
OS   Streptomyces filamentosus NRRL 15998.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE75166.2, ECO:0000313|Proteomes:UP000003986};
RN   [1] {ECO:0000313|Proteomes:UP000003986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RA   Molnar K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000003986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA   Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces roseosporus strain NRRL 15998.";
RL   Submitted (DEC-2008) 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}.
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DR   EMBL; DS999644; EFE75166.2; -; Genomic_DNA.
DR   RefSeq; WP_006125166.1; NZ_DS999644.1.
DR   AlphaFoldDB; D6AJ68; -.
DR   Proteomes; UP000003986; 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:EFE75166.2}.
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        567
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   909 AA;  100975 MW;  ABCA1D05BA1600EC CRC64;
     MSSADQTPAA SPALRADIRR LGDLLGETLV RQEGQELLDL VERVRALTRT DGEAAAELLG
     ETELETAAQL VRAFSTYFHL ANVTEQVHRA HEMRDRRSAE GGLLARTADR LKDADPEHLR
     ETVKNLNVRP VFTAHPTEAA RRSVLNKLRR IAELLETPVI EADRRRLDLR LAENIDLIWQ
     TDELRVVRPE PADEARNAIY YLDELHANAV GDVLEDLAAE LDRVGVELPA GTRPLTFGTW
     IGGDRDGNPN VTPAVTWDVL ILQHEHGITD ALEMIDYLRG LLSNSIRYAG ATEELLTSLQ
     ADLERLPGIS PRYKRLNAEE PYRLKATCIR QKLVNTRERL AEGTPHRPGC DYLGTAELIA
     DLELIQTSLR AHRGGLFADG RMDRTIRTLA AFGLQLATMD VREHADAHHH ALGQLFDRLG
     EESWRYADMP RDYRQKLLAK ELRSRRPLAP TPAPLDAAGE KTLGVFHTIK QAFERFGPEV
     IESYIISMCQ GADDVFAAAV LAREAGLVDL HAGWAKIGIV PLLETTDELK AADHILDEML
     ADPSYRRLVS LRGDVQEVML GYSDSSKFGG ITTSQWEIHR AQRRLRDVAH RYGVRLRLFH
     GRGGTVGRGG GPSHDAILAQ PWGTLEGEIK VTEQGEVISD KYLIPALARE NLELTVAATL
     QASALHTAPR QSDEALARWD AAMDTVSDAA HSAYRKLVED PDLSAYFLAS TPVDQLADLH
     LGSRPARRPG SGVSLDGLRA IPWVFGWTQS RQIVPGWFGV GSGLKALREA GLDTVLDEMH
     EHWHFFRNFI SNVEMTLAKT DLRIARHYVD TLVPDELKHV FDGIEAEHAL TVQEVLRITG
     GEKLLDTNPV LQQTFSIRDA YLDPISYLQV SLLARQRQAA ERGEEPDPLL SRALLLTVNG
     VAAGLRNTG
//
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