ID A0A061P054_9BACL Unreviewed; 445 AA.
AC A0A061P054;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Biotin carboxylase of acetyl-CoA carboxylase {ECO:0000313|EMBL:GAK10293.1};
GN ORFNames=JCM19038_4182 {ECO:0000313|EMBL:GAK10293.1};
OS Geomicrobium sp. JCM 19038.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK10293.1, ECO:0000313|Proteomes:UP000027014};
RN [1] {ECO:0000313|EMBL:GAK10293.1, ECO:0000313|Proteomes:UP000027014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK10293.1,
RC ECO:0000313|Proteomes:UP000027014};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
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:GAK10293.1}.
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DR EMBL; BAXA01000025; GAK10293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061P054; -.
DR eggNOG; COG0439; Bacteria.
DR Proteomes; UP000027014; 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 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000027014}.
FT DOMAIN 1..441
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 445 AA; 49252 MW; 5D74BE9152EEE106 CRC64;
MFKKVLIANR GEIACRIIRT CKEMGIISVA VYSDADATSL HVKIADEAYH IGGSAAKDSY
LNDQKIIEVA KESGAEAIHP GYGFLSENAE FSRLCKENDL VFVGPKPETI EAMGDKISAR
EKMEAAGVPV LPGNHNVASA DEAVEIAATI GYPLMVKAAA GGGGIGMELV TNDDQLRKAY
SSNQRRAKNY FGSGNLYLEK ALLNPRHIEI QVIADSLGDA IHLGERDCSI QRRHQKVIEE
APAPSLCDDV REAMRQAALK AVKSLQYVNA GTLEFLYEEG QFYFLEMNTR LQVEHPVTEA
ITGIDLVKEQ INVASGKELS VRQEEVTFTG HSIECRVYAE DPVTFFPSPG TLSNVLFPRD
VRVDHSIESG TEVTPFYDPM IAKVIVHDLD RQKAIEKMKQ TLLNTSIEGI KTNIPFLRRV
LDQPDFINEN MNTNFVQKHK ETILQ
//
