ID C7M1M3_ACIFD Unreviewed; 772 AA.
AC C7M1M3;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN OrderedLocusNames=Afer_0101 {ECO:0000313|EMBL:ACU53072.1};
OS Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS ICP).
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU53072.1, ECO:0000313|Proteomes:UP000000771};
RN [1] {ECO:0000313|EMBL:ACU53072.1, ECO:0000313|Proteomes:UP000000771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP
RC {ECO:0000313|Proteomes:UP000000771};
RX PubMed=21304635; DOI=10.4056/sigs.1463;
RA Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT (ICP).";
RL Stand. Genomic Sci. 1:38-45(2009).
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670}.
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};
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DR EMBL; CP001631; ACU53072.1; -; Genomic_DNA.
DR AlphaFoldDB; C7M1M3; -.
DR STRING; 525909.Afer_0101; -.
DR KEGG; afo:Afer_0101; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_11; -.
DR Proteomes; UP000000771; Chromosome.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR InterPro; IPR021135; PEP_COase.
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 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ACU53072.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Pyruvate {ECO:0000313|EMBL:ACU53072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000771}.
FT ACT_SITE 37
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 772 AA; 84465 MW; 96356E482370E220 CRC64;
MFNVLNVAEG ADDVTDLAKL APRSLGRIRL TPVLTAHPTE TKRRTILHTL QRIAHAPNAV
DPSDLRLLWF TEELRSRRLE VADEVHTGLF YLTTSLFDAI PVVYRQLAAA RGVDADAIGV
PVRFGSWIGG DRDGNPLVTA EVTKAAFVAN ATACLEAFRS RLDAVKRRLT HSMHFAAVSD
AIVESIRNDE HDFVHLAPYV RTHYVDEPYR QKIYYLLARI DNQLHRLHND PEALDIAPLV
GPDLETALRL IRDSLAAHGD TALAEGPLQD LVWQAATFGT HLASLDIRQE STVHHQAILE
LFGDDPRLAG YWEADADDRL SMLLACLDHP PHARTPRTTL VADLVALFDT LTTVEAELGP
AAIGSYVISM THHAADVIAV LVIARALGAD HLDITPLFET IADLECLESV MEQLFTLPAY
LAHLERRALR QEVMLGYSDS TKDGGMAASA YALYRAQEAL IGLGERHAIT VELFHGRGGT
VGRGGGPIAQ VARAHPRAAL RGTIRITEQG ETISHRYATT DRASATLLTA LGAFGGADDD
TAPTDRAVMV TELVARSSEH AYRALTTSAG FDAYFRSVTP FPELTQLRIG SRPARRHQAD
TGLATIRAIP WVFAWAQSRH TLPAWFGIGT GLATAREAHG DHAIREARAS WPFVAGMLDN
VQIALAKADM RLARRYLDLA DDPTTAAAIF AVIEEEYERT VAETLRATGQ RRLLAWSPTL
ADSLTVRNRV LAELNPLQVT ALGAWRSSRN PDDLTLVLRS INAIATVQKN SG
//
