UniProt/TrEMBL: A0A0H4W6I5

Database: UniProt/TrEMBL
Entry: A0A0H4W6I5_9BORD

LinkDB:  A0A0H4W6I5_9BORD 
Original site:  A0A0H4W6I5_9BORD

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (8)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
Literature (2)   
   PubMed (2)   
All databases (20)   

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ID   A0A0H4W6I5_9BORD        Unreviewed;       948 AA.
AC   A0A0H4W6I5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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:AKQ53731.1};
GN   ORFNames=ACR54_00375 {ECO:0000313|EMBL:AKQ53731.1}, CS347_06250
GN   {ECO:0000313|EMBL:AZW16389.1};
OS   Bordetella hinzii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ53731.1, ECO:0000313|Proteomes:UP000036382};
RN   [1] {ECO:0000313|EMBL:AKQ53731.1, ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|EMBL:AKQ53731.1,
RC   ECO:0000313|Proteomes:UP000036382};
RX   PubMed=26316634;
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT   Humans.";
RL   Genome Announc. 3:e00965-e00915(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA   Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA   Tondella M.L.;
RT   "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000282741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA   Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA   Williams M.M.;
RT   "Whole genome sequencing of various Bordetella species.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AZW16389.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H720 {ECO:0000313|EMBL:AZW16389.1};
RX   PubMed=31744907;
RA   Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA   Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA   Unoarumhi Y., Williams M.M., Tondella M.L.;
RT   "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT   Bordetella Respiratory Pathogens.";
RL   mSystems 4:e00702-19(2019).
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; CP012076; AKQ53731.1; -; Genomic_DNA.
DR   EMBL; CP024172; AZW16389.1; -; Genomic_DNA.
DR   RefSeq; WP_029577999.1; NZ_LT906461.1.
DR   STRING; 103855.ACR54_00375; -.
DR   KEGG; bhz:ACR54_00375; -.
DR   PATRIC; fig|103855.14.peg.354; -.
DR   eggNOG; COG2352; Bacteria.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000036382; Chromosome.
DR   Proteomes; UP000282741; 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:AKQ53731.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036382}.
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        592
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   948 AA;  104939 MW;  FF8D23872AEC856C CRC64;
     MNATRAQSEL AEPLRNDIRL LGRYLGTVIQ ACEGKRVFDT IETLRRSAVR FRREGREEDG
     QLMQQLVKQL RSDDPNLVAR AFSYFLHLFN IAEDRDQNRR QRARALADPA PAPGSLRQAV
     QLLHAQGVSA QRIRRLISEA CVMPVLTAHP TEVQRKSTLD AHREIATLIA QRDQPLTSDE
     SAELDSALLG RVDTLWQTRM LRNTRLTVAD EIENALTYYR STFLSAIPRL YGDLSKLLSP
     EAANPFAPPP APLEPFLRMG SWIGGDRDGN PNVDAGTLEL ALLRQATVVF EHYLNEVHAL
     GAEISVTTLL IDASDALRQL ADAGGDTSPH RRDEPYRRAL IGVYARLAAT ARALTGRELA
     LRSTLPAEPY PHPQALAQDL AVIAESLTRH HGAPIAKLRL AGLQQAVEVF GFHLATLDLR
     QSSDVHERVL TELFARAGQD GRPLRYDLMD EEARVQLLRA ELATARPLAS PWIAYSEDTT
     RELAVLRAAA AARARYGRAA VRQTIVSHTE TLSDLLEVLV LQKETGLIAP AGTAPEAGDG
     LMVVPLFETI PDLERGPSIM AAWLDLPEVR ERVRLAQDES QEVMLGYSDS NKDGGYLTSN
     WSLYRAEREL VEVFRARHVK LRLFHGRGGS VGRGGGSSFD AILAQPPGTV AGQLRLTEQG
     EVIQTKYKDA EIGRWHLELL VSAVLEATLA QQPAAARQAE DAHMAHHGQA MDVLSAGAQR
     SYRKLVYETP GFADYFFAAT PINEIAGLNI GSRPASRKQG QKIEDLRAIP WGFSWAQCRL
     MLTGWYGMGS ALQAYLEDGA EGAPRAKRAR LSQLRDMARD WPAFRTLLSN MEMVLAKSDL
     AIAQRYAMLV PQRGLRERIF GAISEEHART LAMLKLINQR ELLADNPALA ASLRERFAYI
     DPLNYLQIDL LRRHRASQKR PGATPDPRVM PAIHLTINGI AAGLRNSG
//

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