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Database: UniProt
Entry: F8CFH0_MYXFH
LinkDB: F8CFH0_MYXFH
Original site: F8CFH0_MYXFH 
ID   F8CFH0_MYXFH            Unreviewed;       664 AA.
AC   F8CFH0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Acetyl-CoA carboxylase biotin carboxylase subunit {ECO:0000313|EMBL:AEI63580.1};
GN   OrderedLocusNames=LILAB_08345 {ECO:0000313|EMBL:AEI63580.1};
OS   Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI63580.1, ECO:0000313|Proteomes:UP000000488};
RN   [1] {ECO:0000313|EMBL:AEI63580.1, ECO:0000313|Proteomes:UP000000488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX   PubMed=21868801; DOI=10.1128/JB.05516-11;
RA   Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT   "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT   1.";
RL   J. Bacteriol. 193:5015-5016(2011).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP002830; AEI63580.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8CFH0; -.
DR   STRING; 483219.LILAB_08345; -.
DR   KEGG; mfu:LILAB_08345; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_7; -.
DR   Proteomes; UP000000488; 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; 3.30.470.20; 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; 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   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          3..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          122..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          583..659
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   664 AA;  71037 MW;  5EF412EF2CE07FBD CRC64;
     MERFKKVLIA NRGEIAVRVI RTCQRLGYRT VAVFSEADRA APHVLAADEA VAIGPSPAKE
     SYLVIGKILE AAKASGAEAI HPGYGFLSEN ADFARACRDA GLVFIGPEAE AITLMGNKRQ
     AKLRMIAADV PCIPGYEASD LDDEALAVEG ERIGFPLMVK AAAGGGGRGM RLVHEAAQLR
     EALRAARSEA TNAFGSGELI LEKAVIDARH VEVQVFADAH GNVVHLGERD CSVQRRHQKI
     VEESPSPAVS PALRARMGEV AVAAARAIGY RGAGTIEFLL APSGDFYFME MNTRLQVEHP
     VTELITGLDL VEWQLRVAAG ERLPRAQAEV SASGHAIEVR LCAEDPAKGY APQAGRLLTW
     TLPAREGVRI DHGVREGQEI PPFYDSMQAK VIAHGPDRET ARRRLVEALR ELTVFGVTTN
     KNLLLYVLEH AAFRSGEYDT AFIAKHAPAS EVEGLYQADA RARALAAAAL FHDEGLKLAD
     TAGLDASLVN WNTAHRHPVR MKLANRGAEE DVTVQPVSPE AYTVTVGDAS FDVSVLRLSG
     GVLDFSSGGT RGRARYLRDG DTLWLDSGSG AHAVTDVTFR PPSKSDGVGS GRLAAPMDGR
     ILRVDTRVGA AVKPGDVLLV LEAMKMEFQV VADVTGTVAE LNVSVGSQVR AKQLLVALAA
     EKTA
//
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