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Database: UniProt/TrEMBL
Entry: D8IZS4_HERSS
LinkDB: D8IZS4_HERSS
Original site: D8IZS4_HERSS 
ID   D8IZS4_HERSS            Unreviewed;       970 AA.
AC   D8IZS4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
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   ECO:0000313|EMBL:ADJ64414.1};
GN   OrderedLocusNames=Hsero_2925 {ECO:0000313|EMBL:ADJ64414.1};
OS   Herbaspirillum seropedicae (strain SmR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ64414.1, ECO:0000313|Proteomes:UP000000329};
RN   [1] {ECO:0000313|EMBL:ADJ64414.1, ECO:0000313|Proteomes:UP000000329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SmR1 {ECO:0000313|EMBL:ADJ64414.1,
RC   ECO:0000313|Proteomes:UP000000329};
RA   Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA   Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA   Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA   Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA   Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA   Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA   Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA   Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA   Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA   Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA   Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA   Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA   Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA   Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA   Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA   Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA   Weiss V.A., Yates M.A., Souza E.M.;
RT   "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT   fixing, plant-growth promoting beta-Proteobacteria.";
RL   Submitted (APR-2010) 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; CP002039; ADJ64414.1; -; Genomic_DNA.
DR   RefSeq; WP_013234887.1; NC_014323.1.
DR   AlphaFoldDB; D8IZS4; -.
DR   STRING; 757424.Hsero_2925; -.
DR   KEGG; hse:Hsero_2925; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000329; 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; 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:ADJ64414.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000329}.
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        618
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   970 AA;  107904 MW;  5F4EA1FA753D97C5 CRC64;
     MATTNPTKRS ARSAPSTSRS AGANPAATSI TPSKPARGAD KDAPLKEDIR LLGRLLGEVL
     REQEGDEVFE VVETIRQTAV RFRRESDAKA GAELDKLLKK LTRDQTNSVV RAFSYFSHLA
     NIAEDQHHNR RRRAHLLAGS EAQPGSVAYA LSRLDDAGVS GAQVRNFLKE ALVSPVLTAH
     PTEVQRKSIL DAEREIARLV AERDLPLTPR ELRHNTELLR ARIATLWQTR MLRYTKLTVA
     DEIENALSYY RTTFLRELPA LYEDIEAEID SQFPARGKSR PTELPPYVQM GSWIGGDRDG
     NPNVNAGTMQ HALQRQSTVV FDYYLEEVHT LGAELSISTL MVDASPELLA LAATSPDHSE
     HRADEPYRRA LIGIYARLAA TARALGAINI LRQEVGAAAP YETPEQCVAE LDVLVSSLQA
     HHGAALVKPR LAGLKRAVEI FGFHLATLDM RQSSDIHERV LADLFAKAQV EADYAALNEE
     RKIALLLGEL SRPRLLHSPY LEYSEQTDSE LSILRAAREI RRRYGERAIR NYIISHTETL
     SDLLEVLLLQ KETGLLHIEG NQLRELELMV IPLFETIPDL RCAAEIMRGW LSLPQVKGLI
     AKHGKLQEVM LGYSDSNKDG GFLTSNWELY KAENQLVELF NEAGVKLRLF HGRGGTVGRG
     GGPSYQAILA QPPGTVNGQI RLTEQGEIIA SKFANPEIGR RNLELLVAAT LEASLMPTNA
     DDKEARKLAE FERVMEELSE RAYRAYRNLV YETPGFTDYF FAATPIAEIA QLNIGSRPAS
     RKATQRIEDL RAIPWGFSWG QCRLLFPGWY GFGSAVSGWL EDAGNAKEAA RRLATLRAMC
     KEWPFFAALL SNMDMVLSKT DLAVASRYAG LVADRKLRNA IFGRITDEHE RTSAMLSTIT
     GSKERLAANP LLARSIKNRF AYLDPLNHLQ VELIKRHRAT VAAKRTPEER VQRGIHLTIN
     GVAAGLRNTG
//
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