ID I4LUS4_GARVA Unreviewed; 615 AA.
AC I4LUS4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=CGSMWGv55152_01960 {ECO:0000313|EMBL:EIK80714.1};
OS Gardnerella vaginalis 55152.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=698955 {ECO:0000313|EMBL:EIK80714.1, ECO:0000313|Proteomes:UP000005936};
RN [1] {ECO:0000313|EMBL:EIK80714.1, ECO:0000313|Proteomes:UP000005936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55152 {ECO:0000313|EMBL:EIK80714.1,
RC ECO:0000313|Proteomes:UP000005936};
RX PubMed=22609915; DOI=10.1128/JB.00056-12;
RA Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT Consistent with Subspeciation into Genovars.";
RL J. Bacteriol. 194:3922-3937(2012).
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:EIK80714.1}.
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DR EMBL; ADEQ01000005; EIK80714.1; -; Genomic_DNA.
DR RefSeq; WP_004120950.1; NZ_ADEQ01000005.1.
DR AlphaFoldDB; I4LUS4; -.
DR PATRIC; fig|698955.3.peg.384; -.
DR Proteomes; UP000005936; 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 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; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 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}.
FT DOMAIN 4..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 531..607
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 454..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 67174 MW; 1EEE2C29A641F3DC CRC64;
MVTNIKKILV ANRGEIALRV IRTAQEMGIP TVAIYAASDR QAQYVEMADE AYALSGDTYR
DTYLNEDAII DILHKSGADA VHPGYGFLSE VASFAQKVID AGAVWIGPKP EALIDLGDKI
TARRVATRAK VPPVPGISEP VKDIRELLTF AQTHGYPVMM KRTDGGGGRG ITVVHNDDEL
RGFYMNHDAL QGGDLDEYFI ERFIDKARHV ETQVGRDSHG NFTIYSTRDC SVQRRNQKLV
EEAPAPFLTD DENAQLHRYS RNLFEAVDYV GLGTCEYMVT SQHKVYFLEV NPRLQVEHTV
SEEVSGLDLV REQLTIADGG ELTQNHPSRG HSFELRITSE DPATNLTPSA GTLTKIEWPS
GPGIRVDSGV EVGDSVSPKF DSMMGKLIVT AQNRDVAIAR VRRALKELCI EGVPTPAKLF
EQIFNDPDFT AQDHDFDIST KWLERKYLNR TAAAANGGQP ASLDSNKSGE DAQNKPTKME
SFVIEVDNKR VKLTIPQDIV DNLTGSARVR STVRASQPLR GRGLRGDTHK SETPKDAPGV
ISAPMQAVIT RVNVAEGQNV AKGDLLAVLE SMKMENYVYA PAAGVVTGIF VGPGDGVEAG
EKLVTIDVTK GGSAK
//
