ID I9APL9_LACPE Unreviewed; 440 AA.
AC I9APL9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:EIW14872.1};
GN Name=accC1 {ECO:0000313|EMBL:EIW14872.1};
GN ORFNames=KCA1_0502 {ECO:0000313|EMBL:EIW14872.1};
OS Lactiplantibacillus pentosus KCA1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1136177 {ECO:0000313|EMBL:EIW14872.1};
RN [1] {ECO:0000313|EMBL:EIW14872.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCA1 {ECO:0000313|EMBL:EIW14872.1};
RX PubMed=23527145;
RA Anukam K.C., Macklaim J.M., Gloor G.B., Reid G., Boekhorst J., Renckens B.,
RA van Hijum S.A., Siezen R.J.;
RT "Genome Sequence of Lactobacillus pentosus KCA1: Vaginal Isolate from a
RT Healthy Premenopausal Woman.";
RL PLoS ONE 8:E59239-E59239(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EIW14872.1}.
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DR EMBL; AKAO01000015; EIW14872.1; -; Genomic_DNA.
DR RefSeq; WP_003637747.1; NZ_CM001538.1.
DR AlphaFoldDB; I9APL9; -.
DR PATRIC; fig|1136177.4.peg.86; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_9; -.
DR Proteomes; UP000005826; Chromosome.
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:UniProtKB-KW.
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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..438
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 440 AA; 48198 MW; B428B8F0F691604B CRC64;
MFRKLLIANR GEIAVRIIKA CRQLNIQTVA VCSTADRHAG YTRLADEVVC IGPAAASGSY
LNAEAILMAA INTHADAIHP GYGFLAENAD FAAMCAECGI AWIGPQTEQI KLMGDKAQAK
AFARQQQVPV LAGQSIQGLD WPEIKQAATE IGFPLVLKAS YGGGGKGIRV LSDVHELHQQ
LRAARQEAAA SFLNDAMYLE QFLTTARHIE VQVLGTGQDL FILGDRDCSL QLHKQKVLEE
SPASILTAAQ RQKLYDLSRQ LLAGTHYQSL GTIEYLFADG QFYFMEMNTR LQVEHGVTEL
TTGIDIVAEQ IKQAAGVAVA FPEHVGLQPQ CIAIEARLTA TLPVTQTKIE TLQWPEHVRI
DTDYHQGDRL VTMYDGLIAK IMVTGADRLT AVHNLQRALA AVKLQGPATN LDFLRQTAAR
PAYVNDQYTI HSLARWEASK
//
