ID A0A0Q8CK00_9MICO Unreviewed; 321 AA.
AC A0A0Q8CK00;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:KRA11652.1};
GN ORFNames=ASD61_06240 {ECO:0000313|EMBL:KRA11652.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA11652.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA11652.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11652.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA11652.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11652.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRA11652.1}.
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DR EMBL; LMGR01000001; KRA11652.1; -; Genomic_DNA.
DR RefSeq; WP_055819661.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8CK00; -.
DR STRING; 1736567.ASD61_06240; -.
DR Proteomes; UP000051073; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR048764; PylC_PurT_N.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF15632; ATPgrasp_Ter; 1.
DR Pfam; PF21360; PylC-like_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000051073}.
FT DOMAIN 119..288
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 321 AA; 33710 MW; 35C66A40DD8515C3 CRC64;
MTVSRVLVTG AGGPAGVAVI RSLLKRDDLE VFAADMDGWA SALYLVPAER RRIIPAGLAP
EFVDAIIALV ADDGIDVIVS TVDAELPGLA DRRAELGAEL AAPSAEALHT TLDKWLLMQA
VEGKARIPHT ELLTQEGAEY DWVFPVIVKP RSGAGSRGVH LVHTRAELEA AAGDTTQIIQ
ENLPGDEFSV DVILGADGHV ISAVPRLRAR VDSGVAVAGR TVHRAELEDT AAACASAAGL
VGVANVQLRY ATDGTPALLE INPRFSGSMP LTVAAGVDMP SLAVDLALGR ELPQTVPFQE
IAVTRFLEDI FLPVDEIIAS S
//
