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Database: UniProt/TrEMBL
Entry: X8CH68_MYCIT
LinkDB: X8CH68_MYCIT
Original site: X8CH68_MYCIT 
ID   X8CH68_MYCIT            Unreviewed;       938 AA.
AC   X8CH68;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   28-MAR-2018, entry version 31.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:EUA55171.1};
GN   ORFNames=I550_3322 {ECO:0000313|EMBL:EUA55171.1};
OS   Mycobacterium intracellulare 1956.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1299331 {ECO:0000313|EMBL:EUA55171.1, ECO:0000313|Proteomes:UP000020825};
RN   [1] {ECO:0000313|EMBL:EUA55171.1, ECO:0000313|Proteomes:UP000020825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1956 {ECO:0000313|EMBL:EUA55171.1,
RC   ECO:0000313|Proteomes:UP000020825};
RA   Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D.,
RA   DeGroote M.A., Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K.,
RA   Sengamalay N., Fraser C.M., Hine E., Shefchek K.A., Das S.P.,
RA   Tettelin H.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EUA55171.1}.
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DR   EMBL; JAOG01000002; EUA55171.1; -; Genomic_DNA.
DR   RefSeq; WP_014380460.1; NZ_CP009499.1.
DR   EnsemblBacteria; EUA55171; EUA55171; I550_3322.
DR   GeneID; 11909920; -.
DR   KEGG; mie:LG41_15040; -.
DR   PATRIC; fig|1299331.3.peg.3240; -.
DR   KO; K01595; -.
DR   Proteomes; UP000020825; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000020825};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:EUA55171.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:EUA55171.1}.
FT   ACT_SITE    164    164       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    596    596       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   938 AA;  102846 MW;  5BA3EAF6CEDCF0C6 CRC64;
     MADASEAPED TLEPIGAVQR TPVGREATEP MRADIRLLGA ILGDTVREQN GREVFELVER
     ARVESFRVRR SEIDRAELAR MFFRIDIHQA IPVIRAFSHF ALLANVAEDI HRERRRAVHV
     AAGEPPPDST LAATYAKLDE AQLDSDTVAD ALKGAVVAPV ITAHPTETRR RTVFVTQHRI
     TELMRLHAEG HAETDDGRNI ELELRRQVLT LWQTALIRLS RLQITDEIEV GLRYYAAAFF
     KVIPQVNAEV RDALRARWPD ADLFDEPMLQ PGSWIGGDRD GNPNVTADVV RQATGSAAFT
     ALAHYLAELT ALEQELSMSA RLVSVTPALT ELAGGCAEKA RADEPYRRAV RVIRARLSAT
     SAAILDRTPQ QVLDLGLPPY ETPAELGADL DTIDESLRGH GSALLADDRL ALLREGVRVF
     GFHLCGLDMR QNSDAHEEVI CELLAWAGVH PDYRSLPEDE RVELLAAELG TRRPLVADDA
     QLSDLARGEL GVVRAAAHAI KRYGPSAVPN YVISMCRSVS DVLEAAILLK EAGLIDASGP
     EPYCPVGISP LFETIDDLHN GATILHAILE LPIYRALVAA RGETQEVMLG YSDSNKDGGY
     LASSWAVYRA ELALVEVARK TGIRLRLFHG RGGTVGRGGG PSYEAILAQP PGAVNGSLRL
     TEQGEVIAAK YAEPQAAQRN LESLLAATLE STLLDVEGLG DAAEPAYAVL DEVAVLAQRA
     YAELVHDTPG FVDYFMASTP VSEIGSLNIG SRPTSRKPTE SISDLRAIPW VLAWSQSRVM
     LPGWYGTGSA FEQWIAAGPQ SEAERVSILH DLYQRWPFFR SVLSNLAQVL AKSDLGLAAR
     YAELVDDEEL RRRVFDKIVD EHGRTIAMHK LITGQDNLLA DNPALARSVF NRFPYLEPLN
     HLQVELLRRY RSGDDDELVQ RGILLTMNGL ASALRNSG
//
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