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Database: UniProt
Entry: L7LB78_9ACTN
LinkDB: L7LB78_9ACTN
Original site: L7LB78_9ACTN 
ID   L7LB78_9ACTN            Unreviewed;       942 AA.
AC   L7LB78;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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:GAC57298.1};
GN   ORFNames=GOHSU_18_00530 {ECO:0000313|EMBL:GAC57298.1};
OS   Gordonia hirsuta DSM 44140 = NBRC 16056.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1121927 {ECO:0000313|EMBL:GAC57298.1, ECO:0000313|Proteomes:UP000053405};
RN   [1] {ECO:0000313|EMBL:GAC57298.1, ECO:0000313|Proteomes:UP000053405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 16056 {ECO:0000313|EMBL:GAC57298.1,
RC   ECO:0000313|Proteomes:UP000053405};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia hirsuta NBRC 16056.";
RL   Submitted (DEC-2012) 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}.
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:GAC57298.1}.
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DR   EMBL; BANT01000018; GAC57298.1; -; Genomic_DNA.
DR   RefSeq; WP_005939153.1; NZ_BANT01000018.1.
DR   AlphaFoldDB; L7LB78; -.
DR   STRING; 1121927.GOHSU_18_00530; -.
DR   eggNOG; COG2352; Bacteria.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000053405; 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   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:GAC57298.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053405}.
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        605
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   942 AA;  103054 MW;  0AA320E6FA0DBBBF CRC64;
     MPPPESSAEI VARAVATPMI DRIVIDDTGQ AATEPLREDI RFLGGLLGEV IAAHSGEQTF
     DLVENSRRDA FAIRYNEISR DDLAARYTDP TVGELLPVIR AFSSFALLAN LAEDLHRERR
     RRIHQRAGDR PQPSSLAGAL SALRDAGLDD ATVGQALAHG AVVPVITAHP TETRRRTVFE
     AQNTITELMR VRARTELIPE EIERIERQIT EQVLVLWQTA LIRLRRLTIG DEITTGLRYY
     GASFFQVLPN LNRDVRRALT SAYPEAGLEK LSLIRMGSWI GGDRDGNPAV TGQVVNQATS
     AAAATALRHH LNEVTTLRHE LAMSARLVSP ITDDLRALSG RSADDDDEPF RSALRTVRGR
     LAATAQDLLG TDFLLAAERE WAATAEPYAG PEEFLADLDV IDTALRAVVD DTLADNRLGA
     LREAVRTFGF HLSGLDLRQN SEMHEQVVGE LLAWAGVCPD YAGLDEARRV ELLTAELTTR
     RPLTAPDAEL SELAAKELGV VAAAADAVRR FGPEAVPTYI ISMCQSVSDL LEAMVLLKEA
     GLYGLDASGA PRCVVRVVPL LETIEDLQAG ASIITAALDL DFYRALLAGQ QNVQEVMLGY
     SDSNKDGGYL AANWALYRAE LELVQVARQA GLSLRLFHGR GGTVGRGGGP SYDAILAQPP
     GAVQGGLRLT EQGEVIAAKY AEPISARRNL ETLVAATLES TLLDTEGLSD PARAYQVLDE
     LAGLARTAYG DLVHRTPGFV EYFTDSTPLS EIGALNIGSR PTSRKQTTAI SDLRAIPWVL
     SWTQCRVMLP GWYGTGSAFE QWVGDGPERL AQLADYYRQW PFFRSVMSNM AQVLAKSDLG
     LAARYAELVP DADLRERVFT MLATEHERTL RMYAAITGTH DLLADNDALK RSVYNRFPYL
     EPLNLLQVEL LRRFRGGEDT PQIRRAIQLT MNGLATALRN SG
//
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