ID K8GJB8_9CYAN Unreviewed; 1033 AA.
AC K8GJB8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=OsccyDRAFT_3214 {ECO:0000313|EMBL:EKQ68675.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ68675.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ68675.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ68675.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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}.
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:EKQ68675.1}.
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DR EMBL; AJUB01000011; EKQ68675.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GJB8; -.
DR STRING; 864702.OsccyDRAFT_3214; -.
DR PATRIC; fig|864702.5.peg.3439; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_3; -.
DR OrthoDB; 9768133at2; -.
DR Proteomes; UP000001332; 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:EKQ68675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001332}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 681
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1033 AA; 119084 MW; BC45E642FB643257 CRC64;
MSATRSSADD TSSPGTATES RVLPETILTT ASDLFLRLRL KVVEELWESV LRQECGQQLV
DLLNKLRDLC SPEGQAQTFA ETEVLQVVER LDLNEAIRAA RAFALYFQLI NIVEQHYEQR
DQLQYRALVN SDSPLPTHSS AFTPDRGGEE STPASRLEAD LLEKSLHEPT AQRQLGTFHW
LFPKLLSLNV PPQQIQKLIE HLDIWLVFTA HPTEIVRHTI RSKQRRIARI LRQLDRVEER
QAAQGLNIDS VDEEDLRDQL MEEIRLWWRT DELHQFKPTV LDEVDYALHY FQEVLFDVIP
QLYQRMKQAM KASFPGMQPP SSDFCRFGSW VGSDRDGNPS VTHQVTWQTA CYQRNMVLDK
YIQSIRRLIE QLSLSLHWSD VLPELLESLE QDQLQMPELY DQYAVRYRQE PYRLKLTYIQ
KRLENTRDRS LKMYRGEYVQ EEPSDPNKLT YYRSGNEFLR ELRLIQSSLQ ETGLTCRELE
TLIIQVEIYG FHLTHLDIRQ ESTRHSDTVN EIVEYLQILP KSYNELTEAE RVQWLTSELQ
TRRPLIPAEL PFSEKTNETI KTFRIVRKLQ EEFSPAICHT YIISMSHDVS DLLEVLLLAK
EAGLYDPGTG ISTLRVVPLF ETVEDLQKAP AVLTELFELP LYRTMLAGGN AAVQGTSPPD
STWMLTPHLQ EVMLGYSDSN KDSGFLSSNW EIHKAQQALH TLAEKYGVLL RIFHGRGGSV
GRGGGPAYEA ILAQPGRSVN GRIKITEQGE VLASKYSLPE LALYNLEKIT AAVIQGSLLR
TGFDDIQPWH EIMEELAACS RKHYRSLIYE QPDFIDFFHS VTPIEEISQL QISSRPARRG
GKKDLGSLRA IPWVFSWTQS RFLLPAWYGV GTALRDFLYE HPEEHLKLLR YFYFKWPFFK
VVISKVEMTL SKVDLQIARH YMNQLTKPED KPRFEAVFEQ IANEYYLTRE MILAITGHKR
LLDGDPDLQR SVQLRNGTIV PLGFLQVSLL KRLRQYKDEA LSGVVRSRYS KGELLRGALL
TINGIAAGMR NTG
//
