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Database: UniProt
Entry: A0A086ZH93_9BIFI
LinkDB: A0A086ZH93_9BIFI
Original site: A0A086ZH93_9BIFI 
ID   A0A086ZH93_9BIFI        Unreviewed;       945 AA.
AC   A0A086ZH93;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   ORFNames=BBOH_0699 {ECO:0000313|EMBL:KFI45893.1};
OS   Bifidobacterium bohemicum DSM 22767.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437606 {ECO:0000313|EMBL:KFI45893.1, ECO:0000313|Proteomes:UP000029096};
RN   [1] {ECO:0000313|EMBL:KFI45893.1, ECO:0000313|Proteomes:UP000029096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22767 {ECO:0000313|EMBL:KFI45893.1,
RC   ECO:0000313|Proteomes:UP000029096};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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   -!- 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};
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:KFI45893.1}.
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DR   EMBL; JGYP01000002; KFI45893.1; -; Genomic_DNA.
DR   RefSeq; WP_033522256.1; NZ_JGYP01000002.1.
DR   AlphaFoldDB; A0A086ZH93; -.
DR   STRING; 1437606.BBOH_0699; -.
DR   eggNOG; COG2352; Bacteria.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000029096; Unassembled WGS sequence.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   InterPro; IPR021135; PEP_COase.
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; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:KFI45893.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:KFI45893.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029096}.
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..919
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   945 AA;  105300 MW;  3E7F9A97E3534FB4 CRC64;
     MSNQPTSNTS DDARATHPGD TVFTAGVGTK SPEEHELPES LKSDLDLCLD ILRKVLGEYD
     KDLLSTFDTV RGYAVKASAE HYSETIGNAE TKEDNLEKAV KVIDGLNVHD AQLLARAFTT
     YFHLANLCEE NYRVSTLHDR EAEVGENAAT DPVNELTGAY HQLIGEMGPA KAKELLDKLE
     FHPVFTAHPT EARRKAVEGK IRRIATLLSA GKLLGGSDKK ENMRRLYNEV DALFRTSPIA
     LKKPTPVEEA DTILDIFDNT LFNTIPQVYR RFDDWLLGDK AGTVEPQCPA FFHPGSWIGS
     DRDGNPNVTA KVSRTVARKF SDHAISALEN ATRRAGTNLT MEAVTTPPSD ELINLWNHQK
     EMSERLTDKA LLISTQELHR AVMLVMADRL HYTIERDADL MYKSCDDFIA DLKVVQRSLV
     AAGAPRAAYG SLQDVIWQAQ TFGFHLVEME FRQHSLVHSR ALEDIREHGL HGERGELQPM
     THEVLDTFRA LGSIQKRHGQ KAARRYIISF TKSAQNVRDV YELNRMAFAH PEDVPTIDVI
     PLFEQLEDLQ NCVSVLDEMI RIPEVQARLK ATGGRLEVML GYSDSSKDAG PTTATLALHS
     AQGRIAAWAK EHDIDLTLFH GRGGAVGRGG GPANRAVLAQ PVGSVNCRFK LTEQGESIFA
     RYGNQVLAIR HVESVAAATL LQSAPSVEKT NTDMTRKYWD MAQKLDDSAH RRFLDLLNTP
     DFTPWFSTVT PLTEIGLLPI GSRPAKRGLG AKSLDDLRTI PWVFSWAQAR INLAAWYGLG
     TACEEFGDLD TLRAAYREWP VFSTFIDNIE MSLAKTDERI AKMYLALGDR DDLRDKVLEE
     MELTRKWVLS IVGDEWPLQH RHVLGQAVRV RSPYVDALSV TQVLALRRQR MLEAGGGRTL
     PANHEAPKPK KVDNEELSRD QQRSGFTYLI LCTVSGVAAG LQNTG
//
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