ID D2BD79_STRRD Unreviewed; 879 AA.
AC D2BD79;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Sros_1323 {ECO:0000313|EMBL:ACZ84320.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ84320.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ84320.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
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; CP001814; ACZ84320.1; -; Genomic_DNA.
DR RefSeq; WP_012888065.1; NC_013595.1.
DR AlphaFoldDB; D2BD79; -.
DR STRING; 479432.Sros_1323; -.
DR KEGG; sro:Sros_1323; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000002029; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT ACT_SITE 149
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 540
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 879 AA; 96316 MW; 08480FFA0C40E082 CRC64;
MSAIAHHQAE RSSAVTEMPD ELRADVRLLG ELLGQVIAEY GGDDLLADVE RLRKAVIAAR
RGKVSVDEIT AMVAEWPVER AVQIARAFTC YFHLANLAEE HFRIRTLRVR DTGEEPLPES
LAQAVQELGG ERVTELVEGL RLHPVLTAHP TEARRRAVVT AIQRISGQLA AYNSPERGAA
ERAETRRRLL EEIDLLWRTS QLRSTKLDPL DEVRTAMAAF DETLFRVVPL VYRSLDAALG
EGTGTREPLA RPFIRYGSWI GGDRDGNPNV TAKVTRDAVL IQAEHVLIAL ENATHRIART
LTLTAGYTPA SPRLRAALTA AENDHPELVS EMATRSPQEP HRQWLLFVAA RIVATRQRGL
DLAYRSPEEL LGDLRTAQES LVAAGAERQA YGELQHLIWQ VETFGFHLAE LEVRQHSQVH
AAALAELAAG RTSERTDEVL ATIRTIGWIQ ERYGVTACSR YVVSFTRSAD DIAAVYALAG
HALGDKAPQL DVVPLFESGA DLANAPGVLS GMLEIPGIQQ RLAANGRRLE VMLGYSDSAK
ELGPAAATLK LYEAQEALAA WAAEHDVRLT LFHGRGGALG RGGGPANRAV LAQAPGSVGG
RFKVTEQGEV IFARYGHAAI ARRHMEQVTS AVLLASTPSI EARTAEAAGR FRGMAEQVAS
ASEKAYRSLT EAPGFPEWFS LVSPLEEIGS LRLGSRPARR GLGAPRSLDD LRAIPWVFAW
AQTRVNLPGW YGLGSGLQAV ISESGLDELR AAYREWPLFA SLLDNVEMSL AKTDRDIAAR
YLALGGRDDF VEQVLREYDL TRRLVLEITG HSRLLENRRV LSRAVQLRDP YVDALSHLQL
RALSRLRADD GLSEEERERL STLLLLSVNG VAAGLQNTG
//
