ID   A0A077FBU4_9PSED        Unreviewed;       651 AA.
AC   A0A077FBU4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase {ECO:0000313|EMBL:AIL61314.1};
GN   ORFNames=PSAKL28_20930 {ECO:0000313|EMBL:AIL61314.1};
OS   Pseudomonas alkylphenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL61314.1, ECO:0000313|Proteomes:UP000028931};
RN   [1] {ECO:0000313|EMBL:AIL61314.1, ECO:0000313|Proteomes:UP000028931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KL28 {ECO:0000313|EMBL:AIL61314.1,
RC   ECO:0000313|Proteomes:UP000028931};
RA   Lee K., Lim J.Y., Hwang I.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP009048; AIL61314.1; -; Genomic_DNA.
DR   RefSeq; WP_038609924.1; NZ_CP009048.1.
DR   AlphaFoldDB; A0A077FBU4; -.
DR   KEGG; palk:PSAKL28_20930; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_6; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000028931; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.700.40; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR048429; MCC_alpha_BT.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF21139; MCC_alpha_BT; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          5..451
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          124..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          570..649
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   651 AA;  69674 MW;  9DE1345CF2E5DD0A CRC64;
     MTRTPLTTLL VANRGEIACR VMRTAKALGL TTVAVHSAID RDARHSRDAD IRVDLGGAKA
     AESYLDIDKL IAAAKASGAQ AIHPGYGFLS ENAGFARAIE QAGLIFLGPP ASAIDAMGSK
     SAAKALMEQA GVPLVPGYHG EAQDLETFRA AAEKIGYPVL LKATAGGGGK GMKVVESESQ
     LGEALASAKR EAQSSFGDAR MLVEKYVLKP RHVEIQVFAD QHGNCLYLNE RDCSIQRRHQ
     KVVEEAPAPG LSNAQRQAMG EAAVKAAQAI GYVGAGTVEF LLDARGEFFF MEMNTRLQVE
     HPVTEAITGL DLVAWQIRVA CGEPLPITQD QVPLNGHAIE VRLYAEDPAN DFLPATGHLA
     LYRESAPGEG RRVDSGVSEG DSISPFYDPM LGKLIAWGQT REQARLRLLA MLDEFAIGGL
     KTNIAFLRRI LAHPAFASAE LDTGFIPRYQ EQLLPAPQPL PALFWQAAGE AYIQSQPLAP
     RLDDRHSPWA VNSGFRAGVP AQISLHLNSN GQSQALSLTH AAAPALKLAG EQLLIDDNGV
     RRQHLAIRRG ATLYLQWDGE LHAVTPFDPI AEADASHSHQ GGLSAPMNGS IVRVLVEVGQ
     AVEAGTQLVV LEAMKMEHSI RAPQAGTVKA LFCQEGEMVS EGAVLVELEE A
//