ID U3AEM5_9RHOB Unreviewed; 449 AA.
AC U3AEM5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242, 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|ARBA:ARBA00033786, ECO:0000256|RuleBase:RU365063};
GN ORFNames=MBELCI_2186 {ECO:0000313|EMBL:GAD56134.1};
OS Limimaricola cinnabarinus LL-001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1337093 {ECO:0000313|EMBL:GAD56134.1, ECO:0000313|Proteomes:UP000016566};
RN [1] {ECO:0000313|EMBL:GAD56134.1, ECO:0000313|Proteomes:UP000016566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL-001 {ECO:0000313|EMBL:GAD56134.1,
RC ECO:0000313|Proteomes:UP000016566};
RA Nishi S., Tsubouchi T., Takaki Y., Koyanagi R., Satoh N., Maruyama T.,
RA Hatada Y.;
RT "Draft Genome Sequence of Loktanella cinnabarina LL-001T, Isolated from
RT Deep-Sea Floor Sediment.";
RL Genome Announc. 1:e00927-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD56134.1}.
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DR EMBL; BATB01000029; GAD56134.1; -; Genomic_DNA.
DR RefSeq; WP_021694235.1; NZ_BATB01000029.1.
DR AlphaFoldDB; U3AEM5; -.
DR STRING; 1337093.MBELCI_2186; -.
DR eggNOG; COG0439; Bacteria.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000016566; Unassembled WGS sequence.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
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; IPR013815; ATP_grasp_subdomain_1.
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};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, 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..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 449 AA; 48874 MW; 6B57F9688235A698 CRC64;
MFDKILIANR GEIALRVVRA AREMGIKSVA VHSTADSDAM HVRMADEAIC IGPPPSSQSY
LSFPAILSAC EITGAQAIHP GYGFLSENAA FVQAVEDHGL TFIGPSAEHI RMMGDKITAK
DTMKALGVPC VPGSDGGVPS VEAARKVAAE IGYPVIIKAT AGGGGRGMKV AKSEAEIERA
FQTARSESKA AFGNDEVYIE KYLTTPRHIE IQVFGDGKGR AVHLGERDCS LQRRHQKVLE
EAPGPCITQE LRDRIGKVCA DAVAKIKYSG AGTIEFLFEN DEFYFIEMNT RLQVEHPVTE
AIFGVDLVRE QIRVASGLPM SFTQDDLHIR GHAIEVRINA EKLPNFAPCP GRITQYHAPG
GLGVRMDSAL YDGYRIPPYY DSLIAKLIVH GSDRAEALAR LNRALGELIV DGVDTTVPLH
HALLGEPDIL AGNYNIHWLE RWLEQTLQG
//
