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Database: UniProt/TrEMBL
Entry: G7ZHS8_AZOL4
LinkDB: G7ZHS8_AZOL4
Original site: G7ZHS8_AZOL4 
ID   G7ZHS8_AZOL4            Unreviewed;       923 AA.
AC   G7ZHS8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   22-NOV-2017, entry version 39.
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:CBS91106.1};
GN   OrderedLocusNames=AZOLI_p50101 {ECO:0000313|EMBL:CBS91106.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p5 {ECO:0000313|EMBL:CBS91106.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS91106.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p5 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H.,
RA   Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S.,
RA   Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y.,
RA   Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H.,
RA   Gonzalez V., Mavingui P., Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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; FQ311873; CBS91106.1; -; Genomic_DNA.
DR   RefSeq; WP_014249937.1; NC_016624.1.
DR   EnsemblBacteria; CBS91106; CBS91106; AZOLI_p50101.
DR   KEGG; ali:AZOLI_p50101; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000005667; Plasmid AZO_p5.
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:UP000005667};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:CBS91106.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Plasmid {ECO:0000313|EMBL:CBS91106.1};
KW   Pyruvate {ECO:0000313|EMBL:CBS91106.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005667}.
FT   ACT_SITE    152    152       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    585    585       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   923 AA;  102915 MW;  1188312A248D286A CRC64;
     MSAILLQESS ETKDQPLRED IRLLGRILGD TVRSQEGEAV FDIVERIRQT SIRFHREEDQ
     GARKELEAIL NSLSPPQTAR VVRAYSFFSH LANIAEDQHH IRRTRAHALA GSSPRDGTMA
     HALDEATKAG ITTQQLKEFF DSALVSPVLT AHPTEVQRKS ILTVQMAVAK LLAERDHGPM
     TPEEEETNLE SLQRAVLTLW QTAILRATKL AVTDEVANGL TFYDYTFLRE MPRFYAQLED
     HLRRMDPSWA TTELPSFLRM GSWIGGDRDG NPFVTAPVLR QAMRMQSTRA LQFYLDELHT
     LGSELSLSTR VIDVSEPLRQ LAERSPDPSP HRKLEPYRRA ISGIYARVAA TLRTLDGLEA
     PRHAVGDAPP YLTPAELRAD LDIIDRSLTV NGSAALAKGR LRHLRRAVDL FGFHLASIDL
     RQNSDVHERS VAELLSFADA GVDYTSLSED ERIELLVREL ETNRPLASGY ADYSEETSSE
     LDILRTAADA RTRFGSDAVV NCVISKTDGV SDILEVAVLL KEAGLLRPKD KALDLNIAPL
     FETIGDLRNC AATMDRLLSI PTYRRFLESR GNLQEVMLGY SDSNKDGGFL TSGWELYKAE
     IALVEVFAKH GVRLRLFHGR GGSVGRGGGP SYQAILAQPA GAVQGAIRIT EQGEVIAGKY
     SNPEVGRRNL ETLAAATLEA TLLHPESAEP CTDVFLQTME ELSEHAFKAY RGLVYETEGF
     EKYFWESTVI GEIANLNIGS RPASRKKSTS IEDLRAIPWV FSWAQCRLML PGWYGFGSAV
     KAYLAEHPDG MERLRAMHRD WGFFRTLLSN MDMVLSKSNI AIASRYAGLV SDPELRDAIF
     SRIRAEWQDC IEVLLAITEQ SALLEKNPLL ARSIRNRFPY LDPLNHVQVE LLKRHRTSDS
     GEQIARGIHL TINGIAAGLR NSG
//
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