ID A0A0W0W1N3_9GAMM Unreviewed; 651 AA.
AC A0A0W0W1N3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acyl CoA carboxylase subunit alpha {ECO:0000313|EMBL:KTD26141.1};
GN ORFNames=Llan_0036 {ECO:0000313|EMBL:KTD26141.1};
OS Legionella lansingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD26141.1, ECO:0000313|Proteomes:UP000054869};
RN [1] {ECO:0000313|EMBL:KTD26141.1, ECO:0000313|Proteomes:UP000054869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD26141.1,
RC ECO:0000313|Proteomes:UP000054869};
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:KTD26141.1}.
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DR EMBL; LNYI01000001; KTD26141.1; -; Genomic_DNA.
DR RefSeq; WP_028373413.1; NZ_LT906451.1.
DR AlphaFoldDB; A0A0W0W1N3; -.
DR STRING; 45067.Llan_0036; -.
DR PATRIC; fig|45067.4.peg.37; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000054869; 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:UP000054869}.
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 572..649
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 651 AA; 72439 MW; 8255D1140DA15A6B CRC64;
MFNKILIANR GEIACRIMKT CREMGIQTVA IYSTVDKDSL HVTQADSAVC VGEAAAKASY
LNIQAVIDAA KSSGAEAIHP GYGFLSENPL FAKACEEAGI VFIGPSISAM EAMASKQVAK
QLLEKTNVPL TPGYHGSEQS DERLLIEARQ IGFPILLKAA SGGGGKGMRA VHKESEFPEA
LAGARRESMA SFADDTMLIE KLLLNPRHVE IQIMADNHGQ VVHLFERDCS IQRRHQKIIE
EAPAPNLSNS LRQGLAKAAC EVARSIQYRG AGTVEFLVDD NEHFYFMEMN TRLQVEHPVT
EMITGFDLVA WQLKIAANEP LPCSQDQILS RGHAIECRIY AEDPHQGFIP SIGRLHFLKE
PQGQGIRIDS GVRTNSDITM HYDPMIAKLI AWGDNRDQAL QRLRQALEHY AVGGVKTNLP
FLLAICNHPR FVRADLSTNF LAQETIALPH PDKDLALLMA AGYDYLTLTG KKKDPIYQES
FAWQMHLSSH WYWRYLIEEN QEDVKITPID HNSFFLESKE TKAHLRARLI ADQLAIDDGQ
QTRLAFVDDQ MQTITLYFKE GPLSVERFNW QNLDAQSTKK GQLTAPMPAT IVAILKNIGD
KVKEGESLIV LEAMKMEHTI HAPKDGVLAE LFYDVGSQVN EGAELLALKT D
//
