ID A0A0W0U4D1_9GAMM Unreviewed; 651 AA.
AC A0A0W0U4D1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acyl CoA carboxylase subunit alpha {ECO:0000313|EMBL:KTD02609.1};
GN Name=mccA {ECO:0000313|EMBL:KTD02609.1};
GN ORFNames=Lfee_0764 {ECO:0000313|EMBL:KTD02609.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTD02609.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTD02609.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTD02609.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KTD02609.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNYB01000023; KTD02609.1; -; Genomic_DNA.
DR RefSeq; WP_058444050.1; NZ_LNYB01000023.1.
DR AlphaFoldDB; A0A0W0U4D1; -.
DR STRING; 453.Lfee_0764; -.
DR PATRIC; fig|453.4.peg.828; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; 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; 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|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000054698}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 573..650
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 651 AA; 72163 MW; 7431147505D59266 CRC64;
MFNKILIANR GEIACRVIKT ARQMGIHTVA IYSTADKDSQ HVSQADSAFC VGDATAKNSY
LNIEAIIAAA KTSGAQAIHP GYGFLSENPL FAQACADAGI VFVGPSIAAM EAMASKQVAK
QLLEKTGVPL TPGYHGSDQS DERLLQEARQ IGFPVLLKAA SGGGGKGMRA VYKEAEFSQA
LAGARREAMA SFRDDTMLIE KLISNPRHVE VQIMADNYDQ IVHLFERDCS IQRRHQKIIE
EAPAPNLTAT MRQGLAEAAC EVARSIAYRG AGTVEFLVDG DNHFYFMEMN TRLQVEHPVT
EMITGFDLVA WQLKIAANEP LPCPQETIAA HGHALECRIY AEDPQQGFLP SIGQLRFLHE
PTGPGIRIDS GVSLHSHITM HYDPMIAKLI TWGETREQAL QRMRYALANY AVGGVKTNIA
FLQAICRHPR FAKADLSTDF LTQEAINLPL PDERLALLTV ASYDYLVLKN NETDPLRNSS
FAWQMHMSSY WYWRYFIDGQ QQEIKILPLT NTSFKVKISE EEFTLSPRLI ADKLYLDDGQ
QIREILVDNQ GPKITLYLAQ GPLVIERFNW QNFDPQVATK KGQLTAPMPA TVVAILKNKG
DKVKEGESLI VLEAMKMEHT IHAPKDGILA ELFYDVGSQV SEGAELLALK D
//
