ID A0A0S2TDY1_9GAMM Unreviewed; 472 AA.
AC A0A0S2TDY1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242, ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|ARBA:ARBA00033786, ECO:0000256|RuleBase:RU365063};
GN ORFNames=Tel_09495 {ECO:0000313|EMBL:ALP53367.1};
OS Candidatus Tenderia electrophaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Tenderia.
OX NCBI_TaxID=1748243 {ECO:0000313|EMBL:ALP53367.1, ECO:0000313|Proteomes:UP000055136};
RN [1] {ECO:0000313|EMBL:ALP53367.1, ECO:0000313|Proteomes:UP000055136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRL1 {ECO:0000313|EMBL:ALP53367.1};
RA Eddie B.J., Malanoski A.P., Wang Z., Hall R.J., Oh S.D., Heiner C., Lin B.,
RA Strycharz-Glaven S.M.;
RT "Description of Candidatus Tenderia electrophaga gen. nov, sp. nov., an
RT Uncultivated Electroautotroph from a Biocathode Enrichment.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|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|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {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|RuleBase:RU365063}.
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DR EMBL; CP013099; ALP53367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2TDY1; -.
DR STRING; 1748243.Tel_09495; -.
DR KEGG; tee:Tel_09495; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000055136; 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:SF1; BIOTIN CARBOXYLASE; 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}; Pyruvate {ECO:0000313|EMBL:ALP53367.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055136}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 472 AA; 51953 MW; 07DFC3DE56AA3297 CRC64;
MIKKILIANR GEIAVRIVRA CAEMGIKSVA VYTDADRHSL HVKKADEAYN LGPDTVAGYL
NAHRIVNLAV AAGCDALHPG YGFLSENPQL AQICQRRGIK FIGPSADVIR SMGDKIEARS
AMVKAGIPVT PGSDGNVESL EAAVTCAAAV GYPIMLKATS GGGGRGIRRC ENEQALRRNY
DRVISEATKA FGSAEVFIEK CVVNPRHIEA QILADSHGNV IHLFERDCSI QRRHQKLIEI
APSPQLSPEQ REYVGDLAVR AAKAVNYENA GTVEFLLDQD DNFYFMEMNT RLQVEHPVTE
QITGVDIVQE QIRIAAGLKL RFSQDEIKLR GFAMEFRINA EDPKNDFLPS FGRITRYFAP
GGPGVRTDAA IYSGYEIPPY YDSLCAKLTV WALTWDDLLD RAERALNDMG VYGVKTTIPY
HIEIVKSQEF QNGSFDTSFV ENHPELTGYS VKRSPRELAA AIGVAVAAHL GR
//
