ID   A0A0B5DBB3_9CORY        Unreviewed;       521 AA.
AC   A0A0B5DBB3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Acyl-CoA carboxylase subunit beta {ECO:0000313|EMBL:AJE34247.1};
GN   ORFNames=B842_12010 {ECO:0000313|EMBL:AJE34247.1};
OS   Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE34247.1, ECO:0000313|Proteomes:UP000031524};
RN   [1] {ECO:0000313|EMBL:AJE34247.1, ECO:0000313|Proteomes:UP000031524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT   isolated from a wastewater-fed microbial fuel cell.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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DR   EMBL; CP005286; AJE34247.1; -; Genomic_DNA.
DR   RefSeq; WP_040086939.1; NZ_CP005286.1.
DR   AlphaFoldDB; A0A0B5DBB3; -.
DR   STRING; 1223515.B842_12010; -.
DR   KEGG; chm:B842_12010; -.
DR   HOGENOM; CLU_018822_6_2_11; -.
DR   OrthoDB; 4434131at2; -.
DR   Proteomes; UP000031524; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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   3: Inferred from homology;
FT   DOMAIN          1..263
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          263..514
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  56216 MW;  CE61048772C97DDB CRC64;
     MTDTSTARTT TAEKLADLRA RLDQARDPGS ERARARRDEA GQTTPRERIN ALLDEGSFVE
     IGALAKTPGV ADAVYSDGVV TGYGRIDGRP VCIYAHDKTV YGGSVGETFG RKVVEVMEMA
     IKIGCPIIGI QDSGGARIQD AVTSLAMYSE ISRRQLPLSG RSPQISIMLG KSAGGAVYAP
     VTTDFVIAVD GQTEMYVTGP AVIREVTGED VTSAELGGAR QQELNGNISA VLSSEEDAFD
     FVRDLLEHLP LTCHDPAPVF AAPSDEEVSD EAELDSFMPD DSNAGYDMLE LLPLLGDDED
     IVEIQPNYAP NLITAFGRID GRAVGFVANN PMHFAGCIDA DAADKGARFI RICDAYNIPL
     VFVVDTPGYL PGVEQEKAGL IHRGAKLAFA LVEATVPKIT LIVRKAYGGA YAVMGSKNLT
     GDINLAWPTA QIAVMGSAAA VVMIQGKQLE AAPPEQREYL KKIFMDFYDE NMTSPYVAAE
     RGYLDAMIQP RDTRLALRKA IRQMETKVEE DLPKKHTIMP M
//