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Database: UniProt
Entry: D8WS02_9BACT
LinkDB: D8WS02_9BACT
Original site: D8WS02_9BACT 
ID   D8WS02_9BACT            Unreviewed;       172 AA.
AC   D8WS02;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   22-FEB-2023, entry version 34.
DE   SubName: Full=Putative biotin carboxylase {ECO:0000313|EMBL:ADK22941.1};
DE   Flags: Fragment;
GN   Name=accC {ECO:0000313|EMBL:ADK22941.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:ADK22941.1};
RN   [1] {ECO:0000313|EMBL:ADK22941.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20555365; DOI=10.1038/ismej.2010.69;
RA   Alonso-Saez L., Galand P.E., Casamayor E.O., Pedros-Alio C., Bertilsson S.;
RT   "High bicarbonate assimilation in the dark by Arctic bacteria.";
RL   ISME J. 0:0-0(2010).
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DR   EMBL; GU249343; ADK22941.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8WS02; -.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
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; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 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          1..172
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          46..142
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADK22941.1"
FT   NON_TER         172
FT                   /evidence="ECO:0000313|EMBL:ADK22941.1"
SQ   SEQUENCE   172 AA;  18255 MW;  9F867374CEAA90A5 CRC64;
     ADAIHPGYGF LSENAQFADR CFQAGITFIG PSAEAIEIMG NKAAAKKLML STSVPCIPGY
     QDAAQDNKTL IQAAETIGYP VMVKAAAGGG GRGIRLVASA DKFVESVESA RAEAKSAFGS
     DELILEKAVV DARHIEIQII ADTRGNVLHL FERDCSAQRR HQKVIEEAPS PA
//
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