ID A0A5N0UMG8_9PSEU Unreviewed; 598 AA.
AC A0A5N0UMG8;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit {ECO:0000256|ARBA:ARBA00069499};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=FPZ12_041910 {ECO:0000313|EMBL:KAA9150085.1};
OS Amycolatopsis acidicola.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=2596893 {ECO:0000313|EMBL:KAA9150085.1, ECO:0000313|Proteomes:UP000319769};
RN [1] {ECO:0000313|EMBL:KAA9150085.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K81G1 {ECO:0000313|EMBL:KAA9150085.1};
RA Teo W.F.A., Duangmal K.;
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP =
CC N(6)-carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H(+);
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:ARBA00048501};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000256|ARBA:ARBA00048501};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004796}.
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:KAA9150085.1}.
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DR EMBL; VMNW02000125; KAA9150085.1; -; Genomic_DNA.
DR RefSeq; WP_144761233.1; NZ_VMNW02000125.1.
DR AlphaFoldDB; A0A5N0UMG8; -.
DR OrthoDB; 4435847at2; -.
DR Proteomes; UP000319769; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR FunFam; 3.30.470.20:FF:000053; Acetyl-/propionyl-coenzyme A carboxylase alpha chain; 1.
DR FunFam; 2.40.50.100:FF:000003; Acetyl-CoA carboxylase biotin carboxyl carrier protein; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR Gene3D; 2.40.50.100; -; 1.
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; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
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; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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|ARBA:ARBA00023267};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000319769}.
FT DOMAIN 12..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 131..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 522..597
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 504..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 63000 MW; C108318DD4595313 CRC64;
MPEQASGSQG GPVTKILVAN RGEIAVRVIR AAKDAGLTSV AVYADPDRDA PHVQLADEAF
GLGGTTAADS YLVIDKLIDV AKKSGADSVH PGYGFLSENA DFAQAVIDAG LTWIGPSPQA
IRDLGDKVTA RHIATKAGAP LVPGTKDPVA NADEIIAFAN ENGLPVAIKA AFGGGGRGLK
VARTIEEIPE LFESATREAV SAFGRGECFV ERYLDKPRHV EAQVLADKHG NAIVVGTRDC
SLQRRHQKLV EEAPAPFLSD EQRATIHSSA KAICKEAGYS GAGTVEYLVG VDGTISFLEV
NTRLQVEHPV SEETTGLDLV REMFRIARGE KLRFTEDPAP RGHSIEFRIN GEDAGRNFLP
APGTVTKLVF PEGPGVRVDS GVHTGSVVGG SFDSMLAKLI VTGSDRENAL ERSRRALDEL
IVEGMATVVP FHRAIVRDEA FIGDGESFKV HTRWIETEFD NQIEPFTAPG EADEEPAERQ
TLVVEVGGRR LEVSLPGDLA LSGGGGGAAA AKAKPRKRAG GTKTAVSGDA VTAPMQGTIV
KVAVEDGQQV EAGELVVVLE AMKMENPVTA HKAGTVNGLS VEVGSAVTQG SVLLEIKD
//
