ID A0A3S8U1L4_9RHOB Unreviewed; 449 AA.
AC A0A3S8U1L4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Name=accC {ECO:0000313|EMBL:AZL57490.1};
GN ORFNames=EI545_00705 {ECO:0000313|EMBL:AZL57490.1};
OS Tabrizicola piscis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2494374 {ECO:0000313|EMBL:AZL57490.1, ECO:0000313|Proteomes:UP000282002};
RN [1] {ECO:0000313|EMBL:AZL57490.1, ECO:0000313|Proteomes:UP000282002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K13M18 {ECO:0000313|EMBL:AZL57490.1,
RC ECO:0000313|Proteomes:UP000282002};
RA Bae J.-W.;
RT "Complete genome sequencing of Tabrizicola sp. K13M18.";
RL Submitted (DEC-2018) 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|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; CP034328; AZL57490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8U1L4; -.
DR KEGG; taw:EI545_00705; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000282002; 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; 3.40.50.20; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000282002}.
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; 48862 MW; 5672423E12043334 CRC64;
MFEKILIANR GEIALRVIRA CREMGIKSVA VHSTADTDAM HVRMADESVC IGPAPSSESY
LNKAAIISAC EITGAQAVHP GYGFLSENAS FAQALEDHGL TFIGPSAEHI RIMGDKITAK
ETAKALGIPV VPGSEGGVAD FDIAKKAAEE IGFPVIIKAT AGGGGRGMKV AQNAAELEMA
FRTARSEAKN AFGNDEVYIE KYLQKPRHIE IQVFGDGKGR AVHLGERDCS LQRRHQKVFE
EAPGPAITPK MRAEIGAICA NAVAKINYIG AGTVEFLYED GNFYFIEMNT RLQVEHPVTE
YIFGVDLVRE QIRVAAGMGM SFTQDELEIN GHSIEVRINA EKLPNFAPCP GKVRTFHAPG
GLGVRMDSAL YGGYSIPPYY DSLIGKLIVH GRDRPEALAR LKRALGELII DGVDSSVPLF
HMLLAEPEIQ NGEYNIHWLE KWLAVQFGQ
//
