ID   Q4FSL9_PSYA2            Unreviewed;       926 AA.
AC   Q4FSL9;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 128.
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:AAZ18989.1};
GN   OrderedLocusNames=Psyc_1138 {ECO:0000313|EMBL:AAZ18989.1};
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ18989.1, ECO:0000313|Proteomes:UP000000546};
RN   [1] {ECO:0000313|EMBL:AAZ18989.1, ECO:0000313|Proteomes:UP000000546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4
RC   {ECO:0000313|Proteomes:UP000000546};
RX   PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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}.
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DR   EMBL; CP000082; AAZ18989.1; -; Genomic_DNA.
DR   RefSeq; WP_011280411.1; NC_007204.1.
DR   AlphaFoldDB; Q4FSL9; -.
DR   STRING; 259536.Psyc_1138; -.
DR   KEGG; par:Psyc_1138; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000546; 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:AAZ18989.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000546}.
FT   ACT_SITE        143
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        584
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   926 AA;  104975 MW;  2EB051363C178F26 CRC64;
     MTINNHILRE RISLLGSFLG DAISRQTGEQ TLHTIEILRK GFIQQRREPN EAHKQQLIDF
     IASLDNQALK NVIRSFSIYF FLANLSEENY LREQRHTLRM QSEHSWEGSF RRTLLECRER
     NIEPAQMQEL IEQLKFIPVF TAHPTEARRR TTMNLLQSLF THSDALNNFA KNSFAYEQAK
     EQTAQTIDLL WSSDEVRTRK PLVYDEINNG LHYFNASLFN AIPKVYRNIK DAIVEIYPEL
     IDYPLPAFMS FGSWIGGDRD GNPFVTHDTT EMAVLMHADA VLRHYQVLLK KLRRQLIHSD
     TIVTIEPDVY AKIESYIELD RRVFDYNLDD YGNEPYRRLL SLILSKVKAT NYLIQSKGSD
     SEAKKDAYAN PQELLEDLRI IRQSVNTHDT AHGEGLLLDV IRLVKTCGFH LAALDIRQES
     SYHSGVIADI FANAANLPDY QTLNETERQQ WLTRLLEKPG TPLIYTDNLT DKTREQLALM
     NSVATLRKLV GQDTFGSYVI SMTNNASQLL EVLLLMRFAG LCRVDDKGQL SADLPVAPLF
     ETIEDLKNID KILPAVLDNP LYRGLLQHSD NTQEIMLGYS DSSKDGGIIT SAWQLYSAQQ
     TINRIAEEYG IKTRLFHGRG GSVSRGGGST HKAIAAQPAG TLHGQIKVTE QGEVLYAKYA
     NTDTAVFELT MGITGTLKAC SSRFVVQPPE LPQYEALFAR LADVGEQRYR KLTDHTEGFY
     EFYSQATPVA EISLLNIGSR PAHRNKGLPS KTTLRAIPWV FGWSLARFTL PAWYGVGSAL
     DSVKEDEALM KEMNDCWPFF NVFISNIEMA FTKSDMSIAH AYSQLCDDEM LREQIMTAVT
     DEHELTYSGL NSLLNQQSLL SSQQNLSASL EWRNAYLDPT NYIQIELLKR ARQKEASGDA
     NHGDLDVEDP LIRSINALAA GLRNTG
//