ID E2SF92_9ACTN Unreviewed; 930 AA.
AC E2SF92;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 ECO:0000313|EMBL:EFQ82177.1};
GN ORFNames=HMPREF0063_12701 {ECO:0000313|EMBL:EFQ82177.1};
OS Aeromicrobium marinum DSM 15272.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=585531 {ECO:0000313|EMBL:EFQ82177.1, ECO:0000313|Proteomes:UP000003111};
RN [1] {ECO:0000313|EMBL:EFQ82177.1, ECO:0000313|Proteomes:UP000003111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15272 {ECO:0000313|EMBL:EFQ82177.1,
RC ECO:0000313|Proteomes:UP000003111};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (AUG-2010) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFQ82177.1}.
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DR EMBL; ACLF03000011; EFQ82177.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SF92; -.
DR STRING; 585531.HMPREF0063_12701; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR Proteomes; UP000003111; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW Rule:MF_00595}; Kinase {ECO:0000313|EMBL:EFQ82177.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00595};
KW Pyruvate {ECO:0000313|EMBL:EFQ82177.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003111};
KW Transferase {ECO:0000313|EMBL:EFQ82177.1}.
FT ACT_SITE 155
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT ACT_SITE 591
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 930 AA; 102190 MW; 025DB356DA2FED64 CRC64;
MTPEISHADR LPEQNLPADV PQEEVLRSDV RRVADLLGQT LVRQEGQELF DLVERVRVLS
RRRDDEGAAE DRATVHALLD ELPTDTVASL VRAFSVYFNL ANVAEQVARV REVVDRPYGT
GWLDRAVAEI VEDQGPGALA EAFASLDIRT VFTAHPTEVS RRSTLTKIRR IADILGEPSD
DDTVLRRRQD ANLAQLIDLI WQTDPVRRNR PTPLDEARHA VYYLQDILDE TMPTLSADLA
DTLAVHGIRP AATARPLSFG SWIGGDRDGN PNVTPEITRE VLRLQHRIAN RVVTASLDVL
IRELSTSVDL VGVGDDLLAS LEVDLEVLTD LDPRLLSVNA AEPYRLKLSC MRLKLEHTAD
RIAAGAAHVP GHDYADRSEL LADLALVDGS LRAHGGEIVA DRMVADTIRT ASLVGLHLAT
LDVREHADAH HHAVGLLVDR VGEQPVAYAD LDRAARHRLL SVELGSRRPL SPQPPALDEA
AARTYGVFEV IREMHGVFGP EVVESYIVSM SQGADDVLAA AVLAREVGLV DLHSPEPVAR
IGFVPLLETI EEIRRAGDVL DDLLGDPVYR RIVSLRGEVQ EIMLGYSDSN KEGGITTSQW
ELHQAQRSLR DVAARHGVTL RLFHGRGGTV GRGGGPTYDA ILAQPWGVLA GDIKFTEQGE
VISDKYALPV LARENLELSM AAVLTASSLH TESRQPAETL TDWDTTMELV SGRAYAAYRE
LVEDPSLFDY FLASTPVDQL GGLNIGSRPA RRPDSGGDIS GLRAIPWVFG WTQSRQIVPG
WFGVGSGLRA AREAGHEAAL AQMLEQWHFF GTFISNVEMT LAKTDLAVAS HYVSALVPDD
LQHVFDLIRA EHAITVEEVL RVTGEQRLLD HQPALRRTLE IRDTYLQPIS YAQVDLLARS
RQDPDSTDEH LRRALLLTVN GIAAGLRNTG
//
