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Database: UniProt
Entry: K4INP9_BIFAP
LinkDB: K4INP9_BIFAP
Original site: K4INP9_BIFAP 
ID   K4INP9_BIFAP            Unreviewed;       523 AA.
AC   K4INP9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Propionyl-CoA carboxylase beta chain {ECO:0000313|EMBL:AFU72009.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:AFU72009.1};
GN   OrderedLocusNames=BAST_1440 {ECO:0000313|EMBL:AFU72009.1};
OS   Bifidobacterium asteroides (strain PRL2011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU72009.1, ECO:0000313|Proteomes:UP000007006};
RN   [1] {ECO:0000313|EMBL:AFU72009.1, ECO:0000313|Proteomes:UP000007006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRL2011 {ECO:0000313|EMBL:AFU72009.1,
RC   ECO:0000313|Proteomes:UP000007006};
RX   PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA   Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA   Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA   Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA   Ventura M.;
RT   "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT   colonization of the insect gut.";
RL   PLoS ONE 7:E44229-E44229(2012).
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DR   EMBL; CP003325; AFU72009.1; -; Genomic_DNA.
DR   RefSeq; WP_015022445.1; NC_018720.1.
DR   AlphaFoldDB; K4INP9; -.
DR   STRING; 1147128.BAST_1440; -.
DR   GeneID; 41010651; -.
DR   KEGG; bast:BAST_1440; -.
DR   PATRIC; fig|1147128.3.peg.1464; -.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_018822_6_2_11; -.
DR   Proteomes; UP000007006; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR43842:SF4; PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
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:AFU72009.1}.
FT   DOMAIN          7..259
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          264..523
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          22..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  56521 MW;  B028C945D6AC45F8 CRC64;
     MSVTESTLGS QPVRQGIHRA AALAKQAEEH ARDRQHAKGK QTARERLDLL FDKDTFEEVG
     RFAGGDIAGD RAGSAVITGF GLVYGRKVGV YAQDFSVRGG TLGRAEGEKI CRLMDMALRI
     KVPIVAMIDS GGARIQEGVA ALTQYGRIFR KTCQASGFVP QISLILGPCA GGAVYCPALT
     DLIIMTKENS DMFVTGPDVV KAATGETISM DQLGGGYVHN TRSGVAHYLG EDEADAIDYA
     RTVLAYLPAN SGQEPPRYAF ISGHAERQAA KRLATVIPEN DRQPYDVLDV IHAIVDYGEL
     VQVQELYARS IVVGFACLEG RPVGIVANQP MVDAGSLDVE SSEKLARFVR LCDAFNLPVI
     TLVDTPGYKP GSDQEHAGII RRGAKVIYAY ANAQVPMVTI VLRKAFGGSY IVMGSKAIGA
     DLNYAWPSSQ IAVLGAQGAV NIIHRRDLQE AKEAGRDVDE LRNRLAQEYE TSTVNANLSL
     EMGELDGMID PEQTRPVLVQ AMDLLADKQR VRVNDKHHGN QPL
//
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