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Database: UniProt/TrEMBL
Entry: A0A172ZMJ4_9BACL
LinkDB: A0A172ZMJ4_9BACL
Original site: A0A172ZMJ4_9BACL 
ID   A0A172ZMJ4_9BACL        Unreviewed;       931 AA.
AC   A0A172ZMJ4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=AR543_21695 {ECO:0000313|EMBL:ANF98350.1};
OS   Paenibacillus bovis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF98350.1, ECO:0000313|Proteomes:UP000078148};
RN   [1] {ECO:0000313|EMBL:ANF98350.1, ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|EMBL:ANF98350.1,
RC   ECO:0000313|Proteomes:UP000078148};
RA   Wu Z., Gao C., Liu Z., Zheng H.;
RT   "Genome of Paenibacillus bovis sp. nov.";
RL   Submitted (OCT-2015) 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:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
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:SAAS00635168}.
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DR   EMBL; CP013023; ANF98350.1; -; Genomic_DNA.
DR   RefSeq; WP_060536420.1; NZ_CP013023.1.
DR   EnsemblBacteria; ANF98350; ANF98350; AR543_21695.
DR   KEGG; pbv:AR543_21695; -.
DR   KO; K01595; -.
DR   Proteomes; UP000078148; 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   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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000078148};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ANF98350.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078148}.
FT   ACT_SITE    153    153       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    587    587       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   931 AA;  106856 MW;  A310F60BC3394968 CRC64;
     MSELTVNVSK NHSNNLLRRD VRFLGNILGE VLVHQGGQEL LDIVEKIREL SKSLRAVSLP
     EVFEEFKTLI KNLDSDNRHQ VIRAFAVYFQ LVNIAEQNHR IRRKRDYERS AGENVQSGTM
     ENAVQELKNN NFTAEEVEAI FADLSLELVM TAHPTEAMRR AILDIHKRIS EDVKLLDNPT
     LTFREREQLR EKLLNEVITL WQTDELRDRK PTVLDEVRNG MYYFHETLFD VLPELYQELE
     RSLSKHYPEH DWHVPGFLRF GSWIGGDRDG NPSVTAEVTW KTLQMQRKLA IREYQRILRE
     MMQSLSFSTT IIDVSEELLS SIQKDRLHVT IDKIYSWNNE NEPYRIKIAY MLRKLSNIGD
     DSKQGTTERY NDVSELLEDL KVIDKSLRHH YADYVADTYV KKMIRQVELF GFHTATLDVR
     QHSQEHENSL KEILANMEIV EDYSKLQEEE KIELLGKLLS DPRPITSPYF KYSESTEECL
     AVYRTIHKAQ QEFGTNCISS YLISMTQGAS DILEVMVFAK EMGLFRQLAD GSVHCTLQAV
     PLFETIDDLH EAPRIMRQVL DLPAYRKAVA AMNDLHEIML GYSDSNKDGG VVTANWELRL
     ALNNITAMGQ EYSIKLKFFH GRGGALGRGG MSLDRSILAQ PPHTIGGGIK ITEQGEVLSS
     RYSLQGIAYR SLEQAISALI HSATIAKTGE PAGEGNEEWE DIIRGISEVS LDKYQQLIFR
     DPDFMSFFKQ STPLPEVGEL NIGSRPSKRK NSDRFEDLRA IPWVFAWTQS RYLLPAWYAA
     GTGLQHFYQN QPENMAVLQI MYKEFPFFTT LIDTLQMAIA KADLTIAREY AGMCQDDQSR
     ARIFGLIESE FNLTRDLVLQ ITGQQDILDN VPVIQESVRL RNPYVDPLSY LQVQLLSELR
     QIREEGADDP ELLREVLLTI NGIAAGLRNT G
//
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