PCCX_HALMT
ID PCCX_HALMT Reviewed; 88 AA.
AC I3R7F2;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Propionyl-CoA carboxylase, protein PccX subunit {ECO:0000303|PubMed:25398867};
DE Short=PCC {ECO:0000303|PubMed:25398867};
DE EC=6.4.1.3 {ECO:0000269|PubMed:25398867};
GN Name=pccX {ECO:0000303|PubMed:25398867};
GN OrderedLocusNames=HFX_2479 {ECO:0000312|EMBL:AFK20162.1};
GN ORFNames=BM92_13195 {ECO:0000312|EMBL:AHZ23536.1},
GN C439_14194 {ECO:0000312|EMBL:ELZ99711.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|EMBL:AFK20162.1};
RX PubMed=22247127; DOI=10.1128/aem.07114-11;
RA Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT "Identification of the haloarchaeal phasin (PhaP) that functions in
RT polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT mediterranei.";
RL Appl. Environ. Microbiol. 78:1946-1952(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|Proteomes:UP000006469};
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|EMBL:ELZ99711.1};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000312|Proteomes:UP000027075};
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBSTRATE SPECIFICITY,
RP PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=25398867; DOI=10.1128/aem.03167-14;
RA Hou J., Xiang H., Han J.;
RT "Propionyl coenzyme A (propionyl-CoA) carboxylase in Haloferax
RT mediterranei: Indispensability for propionyl-CoA assimilation and impacts
RT on global metabolism.";
RL Appl. Environ. Microbiol. 81:794-804(2015).
CC -!- FUNCTION: Part of the propionyl coenzyme A carboxylase (PCC) complex
CC involved in propionate utilization and in the production of the poly(3-
CC hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which is a water-insoluble
CC biopolymer used as intracellular energy reserve material when cells
CC grow under conditions of nutrient limitation. The complex catalyzes the
CC carboxylation of propionyl-CoA to methylmalonyl-CoA. PCC is also able
CC to catalyze the carboxylation of acetyl-CoA. PccX could be responsible
CC for the interaction of the biotin carboxylase and carboxyltransferase
CC subunits. {ECO:0000269|PubMed:25398867}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-
CC CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456216; EC=6.4.1.3;
CC Evidence={ECO:0000269|PubMed:25398867};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000305|PubMed:25398867}.
CC -!- SUBUNIT: The propionyl coenzyme A carboxylase (PCC) complex is composed
CC of three subunits: PccA (biotin carboxylase and biotin-carboxyl
CC carrier), PccB (carboxyltransferase) and PccX.
CC {ECO:0000269|PubMed:25398867}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking pccB and pccX genes accumulate a
CC high level of propionyl-CoA, which would then inhibit CoA-dependent
CC enzymes such as succinyl-CoA synthetase and could partially inhibit the
CC TCA cycle. Also affected in growth and glucose utilization. Cells are
CC unable to produce PHBV and show morphological abnormalitiess such as a
CC decrease of PHBV granules. {ECO:0000269|PubMed:25398867}.
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DR EMBL; CP001868; AFK20162.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ23536.1; -; Genomic_DNA.
DR EMBL; AOLO01000011; ELZ99711.1; -; Genomic_DNA.
DR RefSeq; WP_004059930.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R7F2; -.
DR STRING; 523841.HFX_2479; -.
DR EnsemblBacteria; AFK20162; AFK20162; HFX_2479.
DR EnsemblBacteria; AHZ23536; AHZ23536; BM92_13195.
DR EnsemblBacteria; ELZ99711; ELZ99711; C439_14194.
DR GeneID; 40157628; -.
DR KEGG; hme:HFX_2479; -.
DR PATRIC; fig|523841.21.peg.2869; -.
DR eggNOG; arCOG04544; Archaea.
DR HOGENOM; CLU_164493_1_0_2; -.
DR OMA; IGAHLHD; -.
DR OrthoDB; 130562at2157; -.
DR BRENDA; 6.4.1.3; 2566.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Ligase.
FT CHAIN 1..88
FT /note="Propionyl-CoA carboxylase, protein PccX subunit"
FT /id="PRO_0000439638"
SQ SEQUENCE 88 AA; 9215 MW; FAB90E85E3ADAB95 CRC64;
MTEDLLSGLS IPDDADSEEA AAIAAAVGAH LHDQTAAAVA AAADEEETWD EKRWQYAGRL
DSVTGCARRV PSGAPTNAWA ASGRTDRF
