ID E6X8Q7_CELAD Unreviewed; 449 AA.
AC E6X8Q7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|RuleBase:RU365063};
GN OrderedLocusNames=Celal_1338 {ECO:0000313|EMBL:ADV48652.1};
OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV48652.1, ECO:0000313|Proteomes:UP000008634};
RN [1] {ECO:0000313|EMBL:ADV48652.1, ECO:0000313|Proteomes:UP000008634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14237 / IC166 / ACAM 630
RC {ECO:0000313|Proteomes:UP000008634};
RX PubMed=21475589; DOI=10.4056/sigs.1543845;
RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL Stand. Genomic Sci. 4:72-80(2010).
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC {ECO:0000256|ARBA:ARBA00003761, ECO:0000256|RuleBase:RU365063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000861,
CC ECO:0000256|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC ECO:0000256|RuleBase:RU365063}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC carrier protein, biotin carboxylase and the two subunits of carboxyl
CC transferase in a 2:2 complex. {ECO:0000256|ARBA:ARBA00011750,
CC ECO:0000256|RuleBase:RU365063}.
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DR EMBL; CP002453; ADV48652.1; -; Genomic_DNA.
DR RefSeq; WP_013550135.1; NC_014934.1.
DR AlphaFoldDB; E6X8Q7; -.
DR STRING; 688270.Celal_1338; -.
DR KEGG; cao:Celal_1338; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_10; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000008634; Chromosome.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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|RuleBase:RU365063};
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 449 AA; 50027 MW; 302CEE01EAE70459 CRC64;
MFKKILIANR GEIALRIIRT CREMGIKTVA VYSKADEESL HVRFADEAVC IGPAPSSESY
LKIPNIIAAA EITNADAIHP GYGFLSENSK FSRICAEHDI KFIGASGDQI DKMGDKATAK
ITMKEAGVPC VPGSDGLLKD VADAKKIAKK MGYPVMIKAT AGGGGKGMRA VWSEDKLEDL
YNSAVQEAKA AFGNGGMYME KLIEEPRHIE IQIVGDQYGK ACHLSERDCS IQRRHQKLTE
ETPSPFMTDK LRDEMGAAAV KAAEFIKYEG AGTIEFLVDK HRNFYFMEMN TRIQVEHPIT
EQVIDYDLIR EQILVAAGVP ISGKNYLPKL HSIECRINAE DPYHDFRPSP GKITTLHTPG
GHGIRLDTHV YSGYTIPSNY DSMIAKLITT AQTREEAINK MKRALDEFVI EGVKTTIPFH
RQLMDHPDYL AGNYTTKFME DFKMDPPKE
//
