PCCB_ROSDO
ID PCCB_ROSDO Reviewed; 510 AA.
AC Q168G2;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Propionyl-CoA carboxylase beta chain {ECO:0000305|PubMed:20725044};
DE EC=6.4.1.3 {ECO:0000269|PubMed:20725044};
GN Name=pccB {ECO:0000312|EMBL:ABG31631.1};
GN OrderedLocusNames=RD1_2028 {ECO:0000312|EMBL:ABG31631.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT FROM
RP RUEGERIA, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF GLY-79 AND ALA-120.
RX PubMed=20725044; DOI=10.1038/nature09302;
RA Huang C.S., Sadre-Bazzaz K., Shen Y., Deng B., Zhou Z.H., Tong L.;
RT "Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme
RT A carboxylase.";
RL Nature 466:1001-1005(2010).
CC -!- FUNCTION: This is one of the 2 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 (PubMed:20725044). Within the holoenzyme, the
CC alpha subunit catalyzes the ATP-dependent carboxylation of the biotin
CC carried by the biotin carboxyl carrier (BCC) domain, while the beta
CC subunit then tranfers the carboxyl group from carboxylated biotin to
CC propionyl-CoA (Probable). {ECO:0000269|PubMed:20725044,
CC ECO:0000305|PubMed:20725044}.
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:20725044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000269|PubMed:20725044};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000305|PubMed:20725044}.
CC -!- SUBUNIT: The holoenzyme is a dodecamer composed of 6 PccA/alpha
CC subunits and 6 PccB/beta subunits. {ECO:0000269|PubMed:20725044}.
CC -!- INTERACTION:
CC Q168G2; Q5LUF3: pccA; Xeno; NbExp=3; IntAct=EBI-9023183, EBI-9023176;
CC -!- DOMAIN: The beta subunit contains the carboxyl transferase (CT) domain.
CC {ECO:0000305|PubMed:20725044}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; CP000362; ABG31631.1; -; Genomic_DNA.
DR RefSeq; WP_011568248.1; NZ_FOOO01000003.1.
DR PDB; 3N6R; X-ray; 3.20 A; B/D/F/H/J/L=1-510.
DR PDBsum; 3N6R; -.
DR AlphaFoldDB; Q168G2; -.
DR SMR; Q168G2; -.
DR DIP; DIP-59244N; -.
DR IntAct; Q168G2; 1.
DR STRING; 375451.RD1_2028; -.
DR EnsemblBacteria; ABG31631; ABG31631; RD1_2028.
DR KEGG; rde:RD1_2028; -.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_018822_6_0_5; -.
DR OMA; PQNNREN; -.
DR OrthoDB; 886663at2; -.
DR UniPathway; UPA00945; UER00908.
DR EvolutionaryTrace; Q168G2; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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 3D-structure; Ligase; Reference proteome.
FT CHAIN 1..510
FT /note="Propionyl-CoA carboxylase beta chain"
FT /id="PRO_0000448577"
FT DOMAIN 1..257
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 261..504
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1..504
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 292..325
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT MUTAGEN 79
FT /note="G->D: Loss of solubility."
FT /evidence="ECO:0000269|PubMed:20725044"
FT MUTAGEN 120
FT /note="A->P: Loss of solubility."
FT /evidence="ECO:0000269|PubMed:20725044"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:3N6R"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:3N6R"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:3N6R"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3N6R"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:3N6R"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 375..388
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 393..402
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 432..439
FT /evidence="ECO:0007829|PDB:3N6R"
FT TURN 442..445
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 449..461
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 465..469
FT /evidence="ECO:0007829|PDB:3N6R"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:3N6R"
FT HELIX 482..491
FT /evidence="ECO:0007829|PDB:3N6R"
FT TURN 492..495
FT /evidence="ECO:0007829|PDB:3N6R"
SQ SEQUENCE 510 AA; 56100 MW; 693077B43EE98CBF CRC64;
MKDILEQLED RRAAARLGGG QKRIDAQHGR GKLTARERVD LLLDEGSFEE FDMFVTHRCT
DFNMQDQKPA GDGVVTGWGT INGRVVYVFS QDFTVLGGSV SETHSKKICK IMDMAMQNGA
PVIGINDSGG ARIQEGVDSL AGYGEVFQRN IMASGVVPQI SMIMGPCAGG AVYSPAMTDF
IFMVKDSSYM FVTGPDVVKT VTNEQVSAEE LGGATTHTRK SSVADAAFEN DVEALAEVRR
LVDFLPLNNR EKPPVRPFFD DPDRIEPSLD TLVPDNPNTP YDMKELIHKL ADEGDFYEIQ
EEFAKNIITG FIRLEGRTVG VVANQPLVLA GCLDIDSSRK AARFVRFCDA FEIPLLTLID
VPGFLPGTSQ EYGGVIKHGA KLLYAYGEAT VPMVTVITRK AYGGAYVVMS SKHLRADFNY
AWPTAEVAVM GAKGATEIIH RGDLGDPEKI AQHTADYEER FANPFVASER GFVDEVIQPR
STRKRVARAF ASLRNKSVQM PWKKHDNIPL
