ID A0A160JI55_9PROT Unreviewed; 923 AA.
AC A0A160JI55;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=A6A40_13150 {ECO:0000313|EMBL:ANC92750.1};
OS Azospirillum humicireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1226968 {ECO:0000313|EMBL:ANC92750.1, ECO:0000313|Proteomes:UP000077405};
RN [1] {ECO:0000313|EMBL:ANC92750.1, ECO:0000313|Proteomes:UP000077405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SgZ-5 {ECO:0000313|EMBL:ANC92750.1,
RC ECO:0000313|Proteomes:UP000077405};
RX PubMed=23264502; DOI=10.1099/ijs.0.046813-0;
RA Zhou S., Han L., Wang Y., Yang G., Zhuang L., Hu P.;
RT "Azospirillum humicireducens sp. nov., a nitrogen-fixing bacterium isolated
RT from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 63:2618-2624(2013).
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}.
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DR EMBL; CP015285; ANC92750.1; -; Genomic_DNA.
DR RefSeq; WP_063635791.1; NZ_CP015285.1.
DR AlphaFoldDB; A0A160JI55; -.
DR STRING; 1226968.A6A40_13150; -.
DR KEGG; ahu:A6A40_13150; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000077405; 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 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:ANC92750.1}.
FT ACT_SITE 152
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 585
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 923 AA; 103038 MW; 7CA2401AD7BD1E2A CRC64;
MSAILLQESS ETKDQPLRED IRLLGRILGD TVRSQEGEAV FDIVERIRQT SIRFHREEDQ
GARKELEAIL NSLSPPQTAR VVRAYSFFSH LANIAEDQHH IRRTRAHALA GSSPRDGTMA
HALDEAAKAG VTTQQLKEFF DGALVSPVLT AHPTEVQRKS ILTVQMEVAK LLAERDHGPM
TPEEEETNLE SLQRAVLTLW QTAILRATKL AVTDEVANGL TFYDYTFLRE MPRFYAQLED
HLRRTDPSWT TTELPSFLRM GSWIGGDRDG NPFVTAPVLR QAMRMQSTRA LQFYLDELHT
LGSELSLSTR VIDVSEPLRQ LAERSPDPSP HRKMEPYRRA ISGIYARVAA TLRTLDGLEA
PRHAVGEAPP YLAPAELRAD LDIIDRSLTV NGSAALAKGR LRHLRRAVDL FGFHLASIDL
RQNSDVHERS VAELLSFADT AVDYKTLSED ERIDLLVREL ETNRPLASRY ADYSEETSSE
LDILRTAADA RARFGSDAVV NCVISKTDGV SDILEVAVLL KEAGLLRPKD KALDLNIAPL
FETIGDLRNC AATMDRLLSI PTYRRFLESR GNLQEVMLGY SDSNKDGGFL TSGWELYKAE
IALVEVFAKH GVRLRLFHGR GGSVGRGGGP SYQAILAQPA GAVQGAIRIT EQGEVIAGKY
SNPEVGRRNL ETLAAATLEA TLLHPESAEP CTDLFLQTME ELSEHAFKAY RGLVYETEGF
EKYFWESTVI GEIANLNIGS RPASRKKSTS IEDLRAIPWV FSWAQCRLML PGWYGFGSAV
KAYLAQHPDG MERLRAMHRD WGFFRTLLSN MDMVLSKSNI AIASRYAGLV SDPDLREAIF
SRIRAEWQDS IEVLLAITEQ SALLEKNPLL ARSIRNRFPY LDPLNHVQVE LLKRHRTSDS
GEQIARGIHL TINGIAAGLR NSG
//
