ID A0A1T4YVW7_9ACTN Unreviewed; 1062 AA.
AC A0A1T4YVW7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acetyl-CoA carboxylase, carboxyltransferase component {ECO:0000313|EMBL:SKB05395.1};
GN ORFNames=SAMN06295964_0924 {ECO:0000313|EMBL:SKB05395.1};
OS Aeromicrobium choanae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736691 {ECO:0000313|EMBL:SKB05395.1, ECO:0000313|Proteomes:UP000191040};
RN [1] {ECO:0000313|EMBL:SKB05395.1, ECO:0000313|Proteomes:UP000191040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9H-4 {ECO:0000313|EMBL:SKB05395.1,
RC ECO:0000313|Proteomes:UP000191040};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR EMBL; LT796768; SKB05395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4YVW7; -.
DR STRING; 1736691.SAMN06295964_0924; -.
DR OrthoDB; 5240504at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000191040; Chromosome i.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR034733; AcCoA_carboxyl_beta.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
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; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Transferase {ECO:0000313|EMBL:SKB05395.1}.
FT DOMAIN 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 113..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 451..529
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 546..816
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 810..1049
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1062 AA; 112192 MW; 15F011B91A717605 CRC64;
MKVLIANRGE IAHRIERAVR ALDWTPQHVH TAEEAGSADP ESYLLPKAGV AGYLDVEAIV
AAAVLTGSDL VHPGYGFLSE SAELARACEA SGLVFVGPEP TTLELFGDKG SAREHALAHG
VPVLDATGRD ASLAEVAALL ERHPAGIMIK AVSGGGGRGM RPVTDAADLA EAYDRCRSEA
ERAFGNASVY AERLLATAKH IEVQVLGDGT GVVTLGEREC SVQRRHQKVI EVAPSPSLTD
AHRERLTTWA KDLTDPLGYR GLATVEFLVN ADLLRRGGPL DAVFIEVNPR LQVEHTVTEE
VTGTDLVRAQ LLVAAGHRLD EAGVPTDVQP RPGVVAIQSR VNAEEVVGGT VVSTTGTVTA
FSAPDGVRVD TGIAAGTVVD GTFDSLLAKV VTVTEGDHAT ACADADAAVA ALRIDGVRTN
VPLLRELLAH DAVRSGEVTT AWLDRLLADR ADTERTTDES GTVTSVMNGT VLAVSVKPGD
TVGPKSPLAT LESMKMEHPV TAGFAGTVTE VLVGAGEQVA AGQPIAVVAP DDTVDHQHAE
DADVDLDHIR PDLAELHDRI ARTRDASRTE AVAKRHARGH LTAREWVDLL VDEGTFTEYG
ALTVAAQRQR RTLDDLMDNT PADGIITGLG TINGDDAGAS RRCAVLAYDY TVLAGTQGYF
NHKKTDRLLE LARDRKLPVV LFAEGGGGRP GDTDTADLLA AGLNVRTFAT MGSLSGVVPT
VGILTGRCFA GNAALLGCCD VIIGTEDANL GMAGPAMIEG GGLGVFTPEQ IGPMSVQAPN
GVVDIVVGDD AEAISVAQRY LSYFQGGRTA WEAADQRRLR HVIGENRKQV YDIRTVIDAL
VDTDSVLELR REFGTGAITA LVRIEGRAYG LVANNPAHLG GAIDADAADK MARFLQLCDA
HGLPVVSLCD TPGFMVGPES EQTATVRHFS RLFVIAAHLK VPMTTIVLRK AYGLGAQAMA
AGGFAQTTAT VSWPTGEIGG MGLEGAVRLG FSKELAAIED EQARAERYEE LVAQHYEAGK
AINGAMKLEL DEVIDPADTR RWIVATLGDW EGEGSHRYVD TW
//
