ID D6B2N8_9ACTN Unreviewed; 928 AA. AC D6B2N8; A0A126Y3B5; A0A2M9SLS9; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 24-JAN-2024, entry version 75. 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:GHI46237.1}; GN ORFNames=C0Q92_11395 {ECO:0000313|EMBL:RZE24541.1}, ScoT_24110 GN {ECO:0000313|EMBL:GHI46237.1}; OS Streptomyces albidoflavus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=1886 {ECO:0000313|EMBL:GHI46237.1, ECO:0000313|Proteomes:UP001051844}; RN [1] {ECO:0000313|EMBL:RZE24541.1, ECO:0000313|Proteomes:UP000292693} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 100770 {ECO:0000313|EMBL:RZE24541.1, RC ECO:0000313|Proteomes:UP000292693}; RA Li Y., Huang Y.; RT "Population genomics insights into the ecological differentiation and RT adaptive evolution in streptomycetes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GHI46237.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NBRC 12854 {ECO:0000313|EMBL:GHI46237.1}; RA Komaki H., Tamura T.; RT "Whole genome shotgun sequence of Streptomyces albidoflavus NBRC 12854."; RL Submitted (SEP-2022) 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, ECO:0000256|HAMAP- CC 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:GHI46237.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BNDZ01000005; GHI46237.1; -; Genomic_DNA. DR EMBL; PKLL01000012; RZE24541.1; -; Genomic_DNA. DR KEGG; salb:XNR_2069; -. DR eggNOG; COG2352; Bacteria. DR Proteomes; UP000292693; Unassembled WGS sequence. DR Proteomes; UP001051844; Unassembled WGS sequence. 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:RZE24541.1}. FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..27 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 154 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 586 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 928 AA; 102753 MW; 4CD7F3940BD18B45 CRC64; MSSADAQATT TSATGRPGPT ETPEPARTTS PELRADIRRL GDLLGEALVR QEGHELLDLV ERVRALTRTD GEAAAELLGG LELEIAAKLV RAFSTYFHLA NVTEQVHRGR ELRARRAEEG GLLARTADRL KDADPEHLRA TVQNLNVRPV FTAHPTEAAR RSVLGKLRRI AELLETPVIE ADRRRHDTRL AENIDLVWQT DELRVVRPEP ADEARNAVYY LDELHAGAVG DVLEDLTAEL ARVGFELPEN SRPLTFGTWI GGDRDGNPNV TPEVTWDVLI LQHEHGINDA LEVVDELRGF LSNSIRYTGA TEELLASLQA DLDHLPEISP RYKRLNAEEP YRLKATCVRQ KLENTKERLA QGTAHQPGRD YLGTAELLTD LTLIQDSLRE HRGGLFADGR MNRTIRTLAA FGLQLATMDV REHADAHHHA LGQLFDRLGE ESWRYADMPR DYRTRLLAKE LRSRRPLAPS PAPLDAAGEK TLNVFHTVRR ALAVFGPEVV ESYIISMCQG ADDVFAAAVL AREAGLIDLH AGWAKIGIVP LLETTDELRA ADVILDEMLA DPSYRLLVSL RGDVQEVMLG YSDSSKFGGI TTSQWEIHRA QRRLRDVAHR YGVRLRLFHG RGGTVGRGGG PSHDAILAQP WGTLEGEIKV TEQGEVISDK YLVPSLAREN LELTVAATLQ ASALHTAPRQ SVEALARWDA AMDTVSEAAH TAYRKLVEDP DLPSYFLAST PVDQLAELHL GSRPSRRPGS GVSLDGLRAI PWVFGWTQSR QIVPGWFGVG SGLKALREAG LDGVLSEMYE HWHFFRNFVS NVEMTLAKTD LRIARHYVDT LVPDELRHVF DLIEAEHALT VAEILRVTGG EELLDSNPVL QQTFAIRDAY LDPISYLQVS LLARQRAAAE RGEDPDPLLS RALLLTVNGV AAGLRNTG //