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Database: UniProt
Entry: I3R7G3
LinkDB: I3R7G3
Original site: I3R7G3 
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   16-JAN-2019, entry version 48.
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;
OC   Haloferacales; 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 /
RC   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 /
RC   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.,
RA   Chen Y., 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 /
RC   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.,
RA   Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea
RT   reveals 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 /
RC   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
RP   SUBUNIT.
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   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
RT   impacts on global metabolism.";
RL   Appl. Environ. Microbiol. 81:794-804(2015).
CC   -!- FUNCTION: Part of the propionyl coenzyme A carboxylase (PCC)
CC       complex involved in propionate utilization and in the production
CC       of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which
CC       is a water-insoluble biopolymer used as intracellular energy
CC       reserve material when cells grow under conditions of nutrient
CC       limitation. The complex catalyzes the carboxylation of propionyl-
CC       CoA to methylmalonyl-CoA. PCC is also able to catalyze the
CC       carboxylation of acetyl-CoA. PccA carries two functions: biotin
CC       carboxyl carrier protein and biotin carboxyltransferase.
CC       {ECO:0000269|PubMed:25398867}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-
CC         methylmalonyl-CoA + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:23720, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57327,
CC         ChEBI:CHEBI:57392, ChEBI:CHEBI:456216; EC=6.4.1.3;
CC         Evidence={ECO:0000269|PubMed:25398867};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
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
CC       degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
CC       {ECO:0000305|PubMed:25398867}.
CC   -!- SUBUNIT: The propionyl coenzyme A carboxylase (PCC) complex is
CC       composed of three subunits: PccA (biotin carboxylase and biotin-
CC       carboxyl carrier), PccB (carboxyltransferase) and PccX.
CC       {ECO:0000269|PubMed:25398867}.
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_CP007551.1.
DR   SMR; I3R7G3; -.
DR   EnsemblBacteria; AFK20173; AFK20173; HFX_2490.
DR   EnsemblBacteria; AHZ23547; AHZ23547; BM92_13250.
DR   EnsemblBacteria; ELZ99722; ELZ99722; C439_14249.
DR   GeneID; 13028647; -.
DR   KEGG; hme:HFX_2490; -.
DR   PATRIC; fig|523841.21.peg.2881; -.
DR   KO; K11263; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 36803at2157; -.
DR   BioCyc; HMED523841:G1HBL-2235-MONOMER; -.
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   Gene3D; 3.30.1490.20; -; 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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    601       Propionyl-CoA carboxylase, biotin
FT                                carboxylase and biotin-carboxyl carrier
FT                                subunit.
FT                                /FTId=PRO_0000439637.
FT   DOMAIN        1    445       Biotin carboxylation.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00969}.
FT   DOMAIN      120    316       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      526    601       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   NP_BIND     148    209       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       275    275       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       287    287       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       287    287       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       289    289       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   MOD_RES     567    567       N6-biotinyllysine. {ECO:0000255|PROSITE-
FT                                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
//
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