ID A0A0W0SD56_9GAMM Unreviewed; 651 AA.
AC A0A0W0SD56;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acyl CoA carboxylase subunit alpha {ECO:0000313|EMBL:KTC81455.1};
GN Name=mccA {ECO:0000313|EMBL:KTC81455.1};
GN ORFNames=Lbru_1975 {ECO:0000313|EMBL:KTC81455.1};
OS Legionella brunensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC81455.1, ECO:0000313|Proteomes:UP000054742};
RN [1] {ECO:0000313|EMBL:KTC81455.1, ECO:0000313|Proteomes:UP000054742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC81455.1,
RC ECO:0000313|Proteomes:UP000054742};
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:KTC81455.1}.
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DR EMBL; LNXV01000029; KTC81455.1; -; Genomic_DNA.
DR RefSeq; WP_058441970.1; NZ_LNXV01000029.1.
DR AlphaFoldDB; A0A0W0SD56; -.
DR STRING; 29422.Lbru_1975; -.
DR PATRIC; fig|29422.6.peg.2105; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000054742; 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}.
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 580..649
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 651 AA; 72197 MW; 17CE7B969F2AE81B CRC64;
MFNKILIANR GEIACRIMKT CRQMGVHTVA IYSTADKDSL HVAQADSAYC VGEATAITSY
LNIEAVIAAA VTSGAQAIHP GYGFLSENPL FAKACEEAGI VFIGPSISAM EAMASKQLAK
QLLEATAVPL TPGYHGSEQT DEQLLIEARR IGFPVLLKAA SGGGGKGMRA VHKEAQFSEA
LAGARREAMA SFADDTMLIE KLILNPRHVE VQIMADNHGQ VVHIFERDCS IQRRHQKIIE
EAPAPNLSAS MRHGLAEAAC EVARLINYRG AGTVEFLVDG DEHFYFMEMN TRLQVEHPVT
EMITGFDLVA WQLKIAANEP LPSSQDKILA KGHAIECRIY AEDPHQNFIP STGQLHFLKE
PHGEGIRIDS GVNINSTITM HYDPMIAKLI AWGESRDEAL QRLQKALENY MIGGVKTNIP
FLQAICKHPR FVNTDLSTDF LSQESIELSV PDMELALLMA ASYDYLALAN KETDPLYQES
FAWQMHLSSH WYWRYIIEGK QEEIKIIPHN RVAFKLVLHE KEFNLHPQLL NDQLALNDGH
QTRLAFVEDR TQTILIYLKE GPVAIERFSW QNLDAQTAKK GQLTAPMPAT IVAILKNIGD
NVKEGDSLIV LEAMKMEHTI HAPKDGVLAE LFYDVGSQVN EGAELLALKT D
//
