ID I0LEB3_9ACTN Unreviewed; 455 AA.
AC I0LEB3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN Name=pycA {ECO:0000313|EMBL:CCH22160.1};
GN ORFNames=MILUP08_40040 {ECO:0000313|EMBL:CCH22160.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH22160.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
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:CCH22160.1}.
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DR EMBL; CAIE01000048; CCH22160.1; -; Genomic_DNA.
DR RefSeq; WP_007454082.1; NZ_HF570108.1.
DR AlphaFoldDB; I0LEB3; -.
DR STRING; 1150864.MILUP08_40040; -.
DR eggNOG; COG0439; Bacteria.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000003448; 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:InterPro.
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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCH22160.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:CCH22160.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448}.
FT DOMAIN 1..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 455 AA; 48505 MW; 8E3FD51D79F6849F CRC64;
MIESLLVANR GEIARRVIRT ARRLGIRAIA VYSEADADLP FVAEADEAVL IGPPNPAQSY
RNVEAILAAA KSTGAQAIHP GYGFLSENAE FARTVEASGL IWVGPGADAI TAMGDKINAR
NLMAAAGVPV APGTTDPAAD LDAAVAAAAA IGYPVMVKAA AGGGGMGMGV AVDEAALRSE
YDKVRAFAER MFGDGSVLIE RYFPRVRHVE VQILGLADGR VVALGERECS VQRRNQKLVE
ESPSPAVSPE LRARLLAAAV RAGEAVGYRN AGTVECLLVP RQRDSEGDGP ATEEFFFLEM
NTRLQVEHPV TEYVYGVDLV EEQLRVAAGL APTFDPDALA PSGHAIELRI NAEDPKRFLP
GPGVVKTWIE PTGVGVRVDS GYTGGNTVTP FYDSLMAKLI LSGDTREQAI ERARTAVAEF
QIEGPKNNLP FFAELLENDE FLDGTYDTGI VSRMR
//
