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Database: UniProt
Entry: Q2RT02_RHORT
LinkDB: Q2RT02_RHORT
Original site: Q2RT02_RHORT 
ID   Q2RT02_RHORT            Unreviewed;       535 AA.
AC   Q2RT02;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Propionyl-CoA carboxylase {ECO:0000313|EMBL:ABC22743.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:ABC22743.1};
GN   OrderedLocusNames=Rru_A1943 {ECO:0000313|EMBL:ABC22743.1};
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22743.1, ECO:0000313|Proteomes:UP000001929};
RN   [1] {ECO:0000313|EMBL:ABC22743.1, ECO:0000313|Proteomes:UP000001929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC   {ECO:0000313|Proteomes:UP000001929};
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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DR   EMBL; CP000230; ABC22743.1; -; Genomic_DNA.
DR   RefSeq; WP_011389696.1; NC_007643.1.
DR   RefSeq; YP_427030.1; NC_007643.1.
DR   AlphaFoldDB; Q2RT02; -.
DR   STRING; 269796.Rru_A1943; -.
DR   EnsemblBacteria; ABC22743; ABC22743; Rru_A1943.
DR   KEGG; rru:Rru_A1943; -.
DR   PATRIC; fig|269796.9.peg.2026; -.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_018822_0_1_5; -.
DR   PhylomeDB; Q2RT02; -.
DR   Proteomes; UP000001929; Chromosome.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR045190; MCCB/AccD1-like.
DR   PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:ABC22743.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001929}.
FT   DOMAIN          22..278
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          278..527
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   535 AA;  57284 MW;  18BBEE3B1FC052A2 CRC64;
     MSVIRSAIDP HGADFRANHL KMTALVDDLK RQVATIKAGG GAAARERHEG RGKLLPRERV
     RALLDIGSPF LEIGQFAAHG VYDDAVPAAG LIAGIGRIEG VDCVVVANDA TVKGGTYYPL
     TVKKHLRAQE IAGENNLPCV YLVDSGGAFL PRQDEVFPDR DHFGRIFYNQ AMLSAAGIPQ
     IAVVMGSCTA GGAYVPAMCD EAIIVRDQGT IFLGGPPLVR AATGEVVSAE DLGGADVHCR
     ISGVTDHYAE DDRHALALAR RVVATLNRTK RVGLALRPPE EPLYDPAELY GIIPTDTRKP
     YDVREVIARL VDGSRLDAFK ALYGPTLVCG FAHVFGYPVG VVANNGILFG DAARKGAHFV
     ELCAKRAIPL IFLQNISGFM VGRKAESAGI ARDGAKMVTA VACARVPKFT VLIGGSFGAG
     NYAMCGRGYG PRLLWSWPNS RISVMGGEQA ATVLAQVRRD ALESQGTPWS EVEEEAFKQP
     LRAQYETQGH PYYASARLWD DGIVDPVDTR MVLGLSISAA LNAPVAETTF GVFRM
//
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