ID A0A1B3MZ30_9SPHN Unreviewed; 900 AA.
AC A0A1B3MZ30;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=BSY17_1718 {ECO:0000313|EMBL:AOF98368.1};
OS Sphingobium sp. RAC03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1843368 {ECO:0000313|EMBL:AOF98368.1, ECO:0000313|Proteomes:UP000094323};
RN [1] {ECO:0000313|EMBL:AOF98368.1, ECO:0000313|Proteomes:UP000094323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC03 {ECO:0000313|EMBL:AOF98368.1,
RC ECO:0000313|Proteomes:UP000094323};
RA Fixen K.R., Hovde B., Kunde Y.A., Davenport K.W., Johnson S.L., Li P.-E.,
RA Xu Y., Daligault H.E., Deodato C.R., Starkenburg S.R., Cattolico R.A.;
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016456; AOF98368.1; -; Genomic_DNA.
DR RefSeq; WP_069065834.1; NZ_CP016456.1.
DR AlphaFoldDB; A0A1B3MZ30; -.
DR STRING; 1843368.BSY17_1718; -.
DR KEGG; sphr:BSY17_1718; -.
DR PATRIC; fig|1843368.3.peg.1761; -.
DR Proteomes; UP000094323; 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:AOF98368.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094323}.
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 567
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 900 AA; 97412 MW; 806FB4906AB109FB CRC64;
MATLSPSPSA PAITQNPDIR FLGRLLGDVI RAYGGESLYK QTEYIRSASV DRARGVQGAD
LTDTGLDVLT LDDTLNFVRG FMLFSMLANL AEDRQGIAAE PGADVASVLA RLESHGIGRD
AVLDLLSHSL IVPVLTAHPT EVRRKSMIDH KNRIADLMLL KDAGRDETED GENLDEAIFR
QIALLWQTRP LRREKLFVAD EIDNVLAYFR DTFLPVLPAL YARWERVLGA RPQSFLRVGS
WIGGDRDGNP FVQAPQLRHA LQRGCQAAIA YYLDALHALG AELSLSTELA HVPQAVLELA
EASGDASPSR GDEPYRRAIS GIYARLAATC TALTGTQPAR PSALKGEAYA MPQDFRRDLV
TVAQGLASEG NGALSSGGAL GRLIRAVETF GFHLATLDMR QNSDVHERVV GELLKVAGVE
PDYATLDEYA RIALLRKELA SNRPLGSRFS AYGEETASEL AIVHAAAEAH RVYGPQCITH
YIISKAESVS DMLEVNILLK EAGLWQAGVD GAPPQAAIMA IPLFETIGDL EAAPAIMSAY
FGLPEIAGVV QARGHQEVMI GYSDSNKDGG YITSTWSLYK ASQALAPVFA DAGAAMQLFH
GRGGAVGRGG GSAFAAIQAQ PRGTVQGRIR ITEQGEMIAA KFGSRDVAMT NLEAMTSATL
LASLEPEGIS ERDAARFTAA MDELSKNAFA AYRDLVYGTE GFKEFFRQLT PIQEISGLKI
GSRPASRTKS NAIEDLRAIP WVFSWAQARV MLPGWYGVGQ ALAGFEDKAL LADMAQHWSF
LKSALANLEM VLAKSDLGIA AQYLPLVEDQ GMADTLFGRI REGWNQTHDG LLAATAQSRL
LEKNAALETS IRLRLPYIEP LNLLQVELLK RHRAGEDDPR IKEGIELSIN AIATALRNSG
//
