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Database: UniProt
Entry: L7LHM6_9ACTN
LinkDB: L7LHM6_9ACTN
Original site: L7LHM6_9ACTN 
ID   L7LHM6_9ACTN            Unreviewed;       950 AA.
AC   L7LHM6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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:GAC59592.1};
GN   ORFNames=GSI01S_03_00510 {ECO:0000313|EMBL:GAC59592.1};
OS   Gordonia sihwensis NBRC 108236.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC59592.1, ECO:0000313|Proteomes:UP000035083};
RN   [1] {ECO:0000313|EMBL:GAC59592.1, ECO:0000313|Proteomes:UP000035083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC59592.1,
RC   ECO:0000313|Proteomes:UP000035083};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
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:GAC59592.1}.
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DR   EMBL; BANU01000003; GAC59592.1; -; Genomic_DNA.
DR   RefSeq; WP_006894842.1; NZ_BANU01000003.1.
DR   AlphaFoldDB; L7LHM6; -.
DR   eggNOG; COG2352; Bacteria.
DR   Proteomes; UP000035083; 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:GAC59592.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035083}.
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        613
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   950 AA;  103516 MW;  5DF77904B79470A9 CRC64;
     MASHSLTPET LARAIATPMV DRISVDDTGR ALTEPLREDI RFLGGLLGEV IRSHAGEATF
     ELVESSRRDA FGIRYAEVTR DQLAGRYDGR AVADLMPVIR AFTNFALLAN LAEDLHRERR
     RRIHQRAGDP APPSSLAATF GKLADAGRTD ADVAAALRSA EVVPVITAHP TETRRRSVFD
     AQNRITELMR VRARTELTPE EDARLTEDIR RQILVLWQTA LIRLRRLTIS DEITTGLRYY
     GASFFDVVPA LNKDVRAALV EAYPDAGLDG LSMISMGSWI GGDRDGNPFV SAEVVDEAAT
     SAARTAMRHH LDELAALHQE LSLSARLFSP VSPALSALGS GFAPPDEPGD TDDEPFRSAV
     SAVRSRVLAR ALRTLGEDAV DPAELDTARA AAPYGDADEF LADLDVIDRA LRAAHDDSIA
     DDRLATLREA VRTFGFHLSG LDMRQNSETH EQVVAELLSW AGVCADYPAL PEADRIGLLT
     AELASRRPLT TPDAELSELA MKELGVVHAA AGAIERFGPR AVPNYVISMC SSVSDLLEVL
     ILLKEAGIYH AAGPGDAGPS CSVRVVPLFE TIEDLRGGAA TLTAALNLGF YRALVRAQGD
     VQEVMLGYSD SNKDGGYLAA NWALYRAELD LVSASRAAEV RLRLFHGRGG TVGRGGGPSY
     DAILAQPPGA VTGSLRLTEQ GEIIAAKYAE PVSARRNLES LLAATIESSL LDVEGLDDPE
     RAYADFDELA ESARRAYSAL VHETPGFVEY FTASTPLSEI GALNIGSRPT SRKQTTAISD
     LRAIPWVLSW TQCRVMLPGW YGVGSAFAQW TGGDDARIAD LRRYYENWPF FRSVMSNMAQ
     VLAKSDMGLA SRYAELVPDE ELRRRVFSMI VEEHERTLEM YTAITGTTDL LADNDALKRS
     VYNRFPYLEP LNLLQVELLQ RFRSGEDSPL IRRGIQLTMN GLATALRNSG
//
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