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Propionyl-CoA carboxylase, biotin carboxylase and biotin-carboxyl carrier subunit (PCC) (EC 6.4.1.3) [Includes: Biotin carboxylase (BC) (EC 6.3.4.14); Biotin-carboxyl carrier protein (BCCP)]

 PCCA_HALMT              Reviewed;         601 AA.
I3R7G3;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
05-SEP-2012, sequence version 1.
30-AUG-2017, entry version 41.
RecName: Full=Propionyl-CoA carboxylase, biotin carboxylase and biotin-carboxyl carrier subunit {ECO:0000303|PubMed:25398867};
Short=PCC {ECO:0000303|PubMed:25398867};
EC=6.4.1.3 {ECO:0000269|PubMed:25398867};
Includes:
RecName: Full=Biotin carboxylase {ECO:0000303|PubMed:25398867};
Short=BC {ECO:0000303|PubMed:25398867};
EC=6.3.4.14 {ECO:0000305|PubMed:25398867};
Includes:
RecName: Full=Biotin-carboxyl carrier protein {ECO:0000303|PubMed:25398867};
Short=BCCP {ECO:0000303|PubMed:25398867};
Name=pccA {ECO:0000303|PubMed:25398867};
Synonyms=accA2 {ECO:0000312|EMBL:AFK20173.1};
OrderedLocusNames=HFX_2490 {ECO:0000312|EMBL:AFK20173.1};
ORFNames=BM92_13250 {ECO:0000312|EMBL:AHZ23547.1},
C439_14249 {ECO:0000312|EMBL:ELZ99722.1};
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=523841;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4;
PubMed=22247127; DOI=10.1128/AEM.07114-11;
Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
"Identification of the haloarchaeal phasin (PhaP) that functions in
polyhydroxyalkanoate accumulation and granule formation in Haloferax
mediterranei.";
Appl. Environ. Microbiol. 78:1946-1952(2012).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4;
PubMed=22843593; DOI=10.1128/JB.00880-12;
Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B.,
Chen Y., Zhou J., Hu S., Xiang H.;
"Complete genome sequence of the metabolically versatile halophilic
archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
hydroxyvalerate) producer.";
J. Bacteriol. 194:4463-4464(2012).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4;
PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
"Phylogenetically driven sequencing of extremely halophilic archaea
reveals strategies for static and dynamic osmo-response.";
PLoS Genet. 10:E1004784-E1004784(2014).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4;
Bautista V.;
"Transcriptional profiles of Haloferax mediterranei on the basis of
nitrogen availability.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, AND
SUBUNIT.
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4;
PubMed=25398867; DOI=10.1128/AEM.03167-14;
Hou J., Xiang H., Han J.;
"Propionyl coenzyme A (propionyl-CoA) carboxylase in Haloferax
mediterranei: Indispensability for propionyl-CoA assimilation and
impacts on global metabolism.";
Appl. Environ. Microbiol. 81:794-804(2015).
-!- FUNCTION: Part of the propionyl coenzyme A carboxylase (PCC)
complex involved in propionate utilization and in the production
of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which
is a water-insoluble biopolymer used as intracellular energy
reserve material when cells grow under conditions of nutrient
limitation. The complex catalyzes the carboxylation of propionyl-
CoA to methylmalonyl-CoA. PCC is also able to catalyze the
carboxylation of acetyl-CoA. PccA carries two functions: biotin
carboxyl carrier protein and biotin carboxyltransferase.
{ECO:0000269|PubMed:25398867}.
-!- CATALYTIC ACTIVITY: ATP + propanoyl-CoA + HCO(3)(-) = ADP +
phosphate + (S)-methylmalonyl-CoA. {ECO:0000269|PubMed:25398867}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000305|PubMed:25398867}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000255|PROSITE-ProRule:PRU00409};
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
-!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA
degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
{ECO:0000305|PubMed:25398867}.
-!- SUBUNIT: The propionyl coenzyme A carboxylase (PCC) complex is
composed of three subunits: PccA (biotin carboxylase and biotin-
carboxyl carrier), PccB (carboxyltransferase) and PccX.
{ECO:0000269|PubMed:25398867}.
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EMBL; CP001868; AFK20173.1; -; Genomic_DNA.
EMBL; AOLO01000011; ELZ99722.1; -; Genomic_DNA.
EMBL; CP007551; AHZ23547.1; -; Genomic_DNA.
RefSeq; WP_004059941.1; NZ_CP007551.1.
SMR; I3R7G3; -.
EnsemblBacteria; AFK20173; AFK20173; HFX_2490.
EnsemblBacteria; AHZ23547; AHZ23547; BM92_13250.
EnsemblBacteria; ELZ99722; ELZ99722; C439_14249.
GeneID; 13028647; -.
KEGG; hme:HFX_2490; -.
PATRIC; fig|523841.21.peg.2881; -.
KO; K11263; -.
OMA; EAPSPIM; -.
OrthoDB; POG093Z0640; -.
UniPathway; UPA00945; UER00908.
Proteomes; UP000006469; Chromosome.
Proteomes; UP000011603; Unassembled WGS sequence.
Proteomes; UP000027075; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004658; F:propionyl-CoA carboxylase activity; IDA:UniProtKB.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR016185; PreATP-grasp_dom.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
ATP-binding; Biotin; Complete proteome; Ligase; Magnesium; Manganese;
Metal-binding; Nucleotide-binding; Reference proteome.
CHAIN 1 601 Propionyl-CoA carboxylase, biotin
carboxylase and biotin-carboxyl carrier
subunit.
/FTId=PRO_0000439637.
DOMAIN 1 445 Biotin carboxylation.
{ECO:0000255|PROSITE-ProRule:PRU00969}.
DOMAIN 120 316 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 526 601 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
NP_BIND 148 209 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
METAL 275 275 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 287 287 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 287 287 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 289 289 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
MOD_RES 567 567 N6-biotinyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
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


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