PCCB_HALMT
ID PCCB_HALMT Reviewed; 516 AA.
AC I3R7F1;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Propionyl-CoA carboxylase, carboxyltransferase subunit {ECO:0000303|PubMed:25398867};
DE Short=PCC {ECO:0000303|PubMed:25398867};
DE EC=6.4.1.3 {ECO:0000269|PubMed:25398867};
GN Name=pccB {ECO:0000303|PubMed:25398867}; Synonyms=accA;
GN OrderedLocusNames=HFX_2478 {ECO:0000312|EMBL:AFK20161.1};
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 [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 [2]
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.
CC {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}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; CP001868; AFK20161.1; -; Genomic_DNA.
DR AlphaFoldDB; I3R7F1; -.
DR SMR; I3R7F1; -.
DR STRING; 523841.HFX_2478; -.
DR EnsemblBacteria; AFK20161; AFK20161; HFX_2478.
DR KEGG; hme:HFX_2478; -.
DR eggNOG; arCOG02705; Archaea.
DR HOGENOM; CLU_018822_6_2_2; -.
DR OMA; PQNNREN; -.
DR BRENDA; 6.4.1.3; 2566.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000006469; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IDA:UniProtKB.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW Ligase; Lyase.
FT CHAIN 1..516
FT /note="Propionyl-CoA carboxylase, carboxyltransferase
FT subunit"
FT /id="PRO_0000439636"
FT DOMAIN 3..259
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 263..509
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 56903 MW; A875B0103A14FC39 CRC64;
MTMEDRIDEL REKREEALKG GGEDRIASQH DKGKMTARER IDYFLDDGTF REFDQFRTHR
NHKFGMEETK LPGDGVITGH GEVDGRTVFV FAHDFTVFGG SLGEVFAEKI CKVMDKAMEV
GAPVIGLNDS AGARIQEGVQ SLGGFGEIFR RNTEASGVVP QISAIMGPCA GGAVYSPALT
DFTFMVRDTS HMFITGPDVI KTVTGEEVTF DELGGATTHT STSGVAHFAT DTEEQALDDI
RHLLSYLPQN NVEDPPRVEP WDDPERVADE LEEIVPDQPR KPYDIHDVLN GVLDEGSFFG
VQEDFAKNIV VGFGRLDGHS VGIVANQPRV NAGTLDIEAS EKGARFIRFC DSFNIPILSF
VDVPGFLPGT DQEHNGIIRH GAKLLYAYSE ATVPLMTVIT RKAYGGAYDV MASKHLGADV
NYAWPTAEIA VMGPQGAVNI LYRDELEAAD DPDARRDELI EEYREEFANP YTAADRGFVD
DVIEPGDTRN RLIADLRMLK SKRKSQPDKK HGNIPL
