ID   B9KIV3_ANAMF            Unreviewed;       515 AA.
AC   B9KIV3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Propionyl-COA carboxylase beta chain (PccB) {ECO:0000313|EMBL:ACM49415.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:ACM49415.1};
GN   Name=pccB {ECO:0000313|EMBL:ACM49415.1};
GN   OrderedLocusNames=AMF_569 {ECO:0000313|EMBL:ACM49415.1};
OS   Anaplasma marginale (strain Florida).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=320483 {ECO:0000313|EMBL:ACM49415.1, ECO:0000313|Proteomes:UP000007307};
RN   [1] {ECO:0000313|EMBL:ACM49415.1, ECO:0000313|Proteomes:UP000007307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Florida {ECO:0000313|EMBL:ACM49415.1,
RC   ECO:0000313|Proteomes:UP000007307};
RX   PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA   Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA   Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT   "Conservation in the face of diversity: multistrain analysis of an
RT   intracellular bacterium.";
RL   BMC Genomics 10:16-16(2009).
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DR   EMBL; CP001079; ACM49415.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9KIV3; -.
DR   STRING; 320483.AMF_569; -.
DR   KEGG; amf:AMF_569; -.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_018822_6_0_5; -.
DR   Proteomes; UP000007307; 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   PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR   PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 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:ACM49415.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007307}.
FT   DOMAIN          7..263
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          267..509
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   515 AA;  56434 MW;  0AE4C8396BF255B1 CRC64;
     MFRYVMCSAV IQELESKKSK LKSGGGVSRV EKQHSKGKLT ARERLEVLLD EGSFQEYGVF
     VEHRSANFGM DKAKISGDGV VTGSGTIYGQ RVCVYSQDFT IFGGSLSEMN SKKICHVMDI
     AAKVGVPVIG INDSGGARIQ EGVDSLAGYG EIFRRNVEMS GVIPQISLIM GSCAGGAVYS
     PALTDFVFMV HGSSCMFVTG PDVIRKVTFE EVTQEDLGGS AVHTKKTGVA DRAFSDEIDA
     LCQIRKFFSF MPANNRSSSR FRETRDAVDR ESESLNTLVP HSSSTPYDMY ELIHKVCDEG
     VFFELKPDFA KNIITGFGRI GGHTVGFVAN QPLHLAGCLD IDASRKAARF VRFCDAFNIP
     IVTLIDVPGF MPGVSQEYSG IIAHGAKLLY AYAEATVPKI SVIVRKAYGG AYIVMNSRHL
     CGDVNYAWPS AEIAVMGSEG AVGIIFRHEK DQECLQRLVQ EYNDKIVNPY VAASRGFIDD
     VIVPSSTRKH LHSALSLLRD KQIARTWRKH DNLPL
//