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Database: UniProt/TrEMBL
Entry: C1AE63_GEMAT
LinkDB: C1AE63_GEMAT
Original site: C1AE63_GEMAT 
ID   C1AE63_GEMAT            Unreviewed;       933 AA.
AC   C1AE63;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   28-MAR-2018, entry version 63.
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:BAH40790.1};
GN   OrderedLocusNames=GAU_3748 {ECO:0000313|EMBL:BAH40790.1};
OS   Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS   100505).
OC   Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC   Gemmatimonas.
OX   NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH40790.1, ECO:0000313|Proteomes:UP000002209};
RN   [1] {ECO:0000313|Proteomes:UP000002209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC   {ECO:0000313|Proteomes:UP000002209};
RA   Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y.,
RA   Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S.,
RA   Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT   "Complete genome sequence of Gemmatimonas aurantiaca T-27 that
RT   represents a novel phylum Gemmatimonadetes.";
RL   Submitted (MAR-2006) 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}.
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DR   EMBL; AP009153; BAH40790.1; -; Genomic_DNA.
DR   RefSeq; WP_015895557.1; NC_012489.1.
DR   STRING; 379066.GAU_3748; -.
DR   EnsemblBacteria; BAH40790; BAH40790; GAU_3748.
DR   KEGG; gau:GAU_3748; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; GAUR379066:G1G2N-3825-MONOMER; -.
DR   Proteomes; UP000002209; 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   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:UP000002209};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:BAH40790.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:BAH40790.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002209}.
FT   ACT_SITE    157    157       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    590    590       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   933 AA;  103267 MW;  B7BF71A4093B98FE CRC64;
     MTDILDPPPA RDEKDRPLRD DIRLLGRLLG DAVREQEGAD VFQLVEDTRR AAIRFAREGR
     AEDREALHVL LDPLPPDTML SVVRAFSYFL QLANIAEDTH RGRRRRAHEV MGSRPREGTL
     EFALEMVRQA IGNDGLAQER LTAFFRSALV SPVLTAHPTE VQRQSTLTVM QQIATLLEQR
     DRMVLTGEER TESDALLTRL VLTLWHTRIV RGERLRVVDE VKNGIAYFRS TFFTEVPRLH
     ANLEDLLSAQ FPGSTWQLTP FLQPGSWIGG DRDGNPFVTA DVLHETLRLQ ASATFDFYLQ
     EIHALGQQLS LSRTLHAVTP ALEALAARSP DTSAQRLDEP YRRALSGIYA RVASTMSGLE
     LPPPVRAALG SGEPYASADA LYDDLVIIRD ALTTTGVGLL AAGRLRRLLM AVQGFGFHLA
     PLDLRQNADV HERVVTELFA QAGVCDNYAA LDESQRVALL ARELEGTRPL HSPHLRYSEE
     VAGELAIVFT AARLRQRYGA SALPHYVISK CDGVSDLLEV ALMLKEAGLA TGGQQATLGL
     DIVPLFETIA DLRRAGDTMR AALALPVYRA LLRTRGDVQE VMLGYSDSNK DGGFLTSGWE
     LYQAQTALMQ AFGDAGVQLR FFHGRGGSVG RGGGPSYDAI LAQPAGAVTG QIRLTEQGEV
     IASKYATPDV GRRNLELLVA ATLEATLTDH ESGADQVTAF RPVMERLSAH AYAAYRALVY
     ETPGFAQYFR ESTPLAEIAT LNIGSRPASR KPSDRIEDLR AIPWVFAWAQ CRCMLPGWYG
     FGSAVTAWLV EQPDGLPVLQ RMAQHWPFFR TLLSNVDMVL AKSDLRVASR YSELVQDETL
     RRTIFAAIEA EWHRTRDALR QITGQDQLLA DNPLLVRSMA NRFPYMDPLN HLQIALLQRH
     REHVASGTAP DDLMRRGIHI TINGIAAGLR NSG
//
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