ID M0JU40_9EURY Unreviewed; 616 AA.
AC M0JU40;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acetyl-CoA carboxylase biotin carboxylase subunit {ECO:0000313|EMBL:QUJ70996.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:QUJ70996.1};
DE SubName: Full=Carbamoyl phosphate synthase L chain {ECO:0000313|EMBL:EMA12677.1};
GN ORFNames=C436_13020 {ECO:0000313|EMBL:EMA12677.1}, KDQ40_09685
GN {ECO:0000313|EMBL:QUJ70996.1};
OS Haloarcula sinaiiensis ATCC 33800.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA12677.1, ECO:0000313|Proteomes:UP000011659};
RN [1] {ECO:0000313|EMBL:EMA12677.1, ECO:0000313|Proteomes:UP000011659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA12677.1,
RC ECO:0000313|Proteomes:UP000011659};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [2] {ECO:0000313|EMBL:QUJ70996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ70996.1};
RA Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT Haloarcula sinaiiensis.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AOLR01000021; EMA12677.1; -; Genomic_DNA.
DR EMBL; CP073366; QUJ70996.1; -; Genomic_DNA.
DR RefSeq; WP_004963494.1; NZ_CP073366.1.
DR AlphaFoldDB; M0JU40; -.
DR GeneID; 64823227; -.
DR KEGG; hsin:KDQ40_09685; -.
DR PATRIC; fig|662476.7.peg.2603; -.
DR OrthoDB; 31083at2157; -.
DR Proteomes; UP000011659; Unassembled WGS sequence.
DR Proteomes; UP000682967; 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 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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:QUJ70996.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..330
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 539..616
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 67490 MW; 892455A5383F4F7B CRC64;
MFDKVLVANR GEIAVRVMRA CEELGIGTVA VYSDADKHAG HVRYADEAYN VGPARAADSY
LDQEAIIDAA KQADADAIHP GYGFLAENAD FAARVQQTDG VTWVGPESES MEALGEKTKA
RKIMQSADVP IVPGTTDPVE DPEEVVEFGE ENGFPVAIKA EGGGGGRGMK IVHDPEEAEE
QLESAKREGE AYFSNDSVYL ERYLENPRHI EVQIIADHHG NVRHLGERDC SLQRRHQKVI
EEGPSPALND ALREKIGDAA RRGVRESDYY NAGTVEFLVE EDTDREQGEL LGEEANFYFL
EVNTRIQVEH CVTEEITDID IVKWQLRVAM DEEITFDQDD VEIEGHAMEF RINAENAADD
FAPATGGSLD TYDPPGGIGV RLDDALRQGD DLVTDYDSMI AKLITYGGDR EECIERGKRA
LKDFDIEGIP TVVPFHRLML TDEKFVNGTH TTKYLDEHLD RTRIEEAQEQ WGTVTESDGE
GDEDEEVVER EFTVEVNGKR FQVDLEERGA PPINVGNVDA DGGSQPQRPQ GGSSSDSGGG
SATTAEGQEV AAEMQGTILE VNVEEGDEVE AGDVLCVLEA MKMENDIVAE RGGTVNDVAV
SEGESVDMGD LLFVIG
//
