ID W8VZL7_9FLAO Unreviewed; 387 AA.
AC W8VZL7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Biotin carboxylase of acetyl-CoA carboxylase {ECO:0000313|EMBL:BAO54796.1};
GN ORFNames=NMS_0787 {ECO:0000313|EMBL:BAO54796.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO54796.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO54796.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO54796.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
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DR EMBL; AP014548; BAO54796.1; -; Genomic_DNA.
DR AlphaFoldDB; W8VZL7; -.
DR STRING; 1454201.NMS_0787; -.
DR HOGENOM; CLU_000395_3_2_10; -.
DR Proteomes; UP000031760; 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: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; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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; 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}.
FT DOMAIN 1..382
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 58..255
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 387 AA; 43125 MW; 950DF3D4CCB70346 CRC64;
MSNIISAAEI TNADAIHPGY GFLSENADFS RICEEHKIKF IGASPDMIAK MGDKATAKAT
MKAAGVPCVP GSDGIIEDFD DCVKVAKETG YPVMLKATAG GGGKGMRAVW SEDKLKAAWD
SARQESKAAF GNDDMYMEKL IEEPRHIEIQ VVGDSYGKAC HLSERDCSVQ RRHQKLTEEV
PSPFMTKKLR KDMGEAAVRA AEFIAYEGAG TVEFLVDKHR NFYFMEMNTR IQVEHPITEQ
VIDFDLIREQ ILVAAGTKIS GKNYEPSLHS IECRINAEDP YHDFRPSPGK ITTLHAPGGH
GVRLDTHVYA GYSIPPNYDS MIAKLITTAR TRQEAIDKMK RALDEFVIEG VKTTIPFHRQ
LMDEPAYVKG EYTTAFMNTF KMKPQED
//
