ID PCCA_HALMT Reviewed; 601 AA.
AC I3R7G3;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Propionyl-CoA carboxylase, biotin carboxylase and biotin-carboxyl carrier subunit {ECO:0000303|PubMed:25398867};
DE Short=PCC {ECO:0000303|PubMed:25398867};
DE EC=6.4.1.3 {ECO:0000269|PubMed:25398867};
DE Includes:
DE RecName: Full=Biotin carboxylase {ECO:0000303|PubMed:25398867};
DE Short=BC {ECO:0000303|PubMed:25398867};
DE EC=6.3.4.14 {ECO:0000305|PubMed:25398867};
DE Includes:
DE RecName: Full=Biotin-carboxyl carrier protein {ECO:0000303|PubMed:25398867};
DE Short=BCCP {ECO:0000303|PubMed:25398867};
GN Name=pccA {ECO:0000303|PubMed:25398867};
GN Synonyms=accA2 {ECO:0000312|EMBL:AFK20173.1};
GN OrderedLocusNames=HFX_2490 {ECO:0000312|EMBL:AFK20173.1};
GN ORFNames=BM92_13250 {ECO:0000312|EMBL:AHZ23547.1},
GN C439_14249 {ECO:0000312|EMBL:ELZ99722.1};
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;
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;
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;
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;
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, SUBSTRATE SPECIFICITY, 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: This is one of the subunits of the biotin-dependent
CC propionyl-CoA carboxylase (PCC), the enzyme catalyzing the
CC carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-
CC CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit
CC catalyzes the ATP-dependent carboxylation of the biotin carried by the
CC biotin carboxyl carrier (BCC) domain, while the beta subunit then
CC transfers the carboxyl group from carboxylated biotin to propionyl-CoA
CC (By similarity). Propionyl-CoA carboxylase is involved in propionate
CC utilization and in the production of the poly(3-hydroxybutyrate-co-3-
CC hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as
CC intracellular energy reserve material when cells grow under conditions
CC of nutrient limitation (PubMed:25398867). Propionyl-CoA carboxylase is
CC also able to catalyze the carboxylation of acetyl-CoA
CC (PubMed:25398867). {ECO:0000250|UniProtKB:Q5LUF3,
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000305|PubMed:25398867};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000305|PubMed:25398867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000305|PubMed:25398867};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
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 -!- DOMAIN: Consists of an N-terminal biotin carboxylation/carboxylase (BC)
CC domain that catalyzes the transient carboxylation of the biotin
CC covalently attached to the C-terminal biotinyl-binding/biotin carboxyl
CC carrier (BCC) domain. {ECO:0000250|UniProtKB:Q5LUF3}.
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DR EMBL; CP001868; AFK20173.1; -; Genomic_DNA.
DR EMBL; AOLO01000011; ELZ99722.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ23547.1; -; Genomic_DNA.
DR RefSeq; WP_004059941.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R7G3; -.
DR SMR; I3R7G3; -.
DR STRING; 523841.HFX_2490; -.
DR PaxDb; 523841-HFX_2490; -.
DR GeneID; 40157617; -.
DR KEGG; hme:HFX_2490; -.
DR PATRIC; fig|523841.21.peg.2881; -.
DR eggNOG; arCOG01591; Archaea.
DR HOGENOM; CLU_000395_3_6_2; -.
DR OrthoDB; 31083at2157; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IDA:UniProtKB.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biotin; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..601
FT /note="Propionyl-CoA carboxylase, biotin carboxylase and
FT biotin-carboxyl carrier subunit"
FT /id="PRO_0000439637"
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 526..601
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 495..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 347
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:Q5LUF3"
FT MOD_RES 567
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 601 AA; 65508 MW; AD350BB97B28A2A8 CRC64;
MFSKVLVANR GEIAVRVMRA CEELGVRTVA VYSEADKHGG HVRYADEAYN IGPARAADSY
LDHESVIEAA RKADADAIHP GYGFLAENAE FARKVEDSEF TWVGPSADAM ERLGEKTKAR
SLMQDADVPV VPGTTEPADS AEDVKAVADD YGYPVAIKAE GGGGGRGLKV VHSEDEVDGQ
FETAKREGEA YFDNASVYVE KYLEAPRHIE VQILADEHGN VRHLGERDCS LQRRHQKVIE
EAPSPALSED LRERIGEAAR RGVRAAEYTN AGTVEFLVED GEFYFMEVNT RIQVEHTVTE
EVTGLDVVKW QLRVAAGEEL DFSQDDVEIE GHSMEFRINA EAPEKEFAPA TGTLSTYDPP
GGIGIRMDDA VRQGDEIGGD YDSMIAKLIV TGSDREEVLV RAERALNEFD IEGLRTVIPF
HRLMLTDEAF REGSHTTKYL DEVLDPERIE AAVERWSPEA VAGDEEEGEV TERTFTVEVN
GKRFEVSLEE RGAPAIPLGG ASAAASASKP SGPRKRREES DEGGQQVIEG DGESVAAEMQ
GTILAVEVDE GDDVEPGDTV CILEAMKMEN DVVAERGGTV SQVLVGEGDS VDMGDVLLVL
E
//
