ID M0D8X4_9EURY Unreviewed; 622 AA.
AC M0D8X4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:ELZ31945.1};
GN ORFNames=C473_10583 {ECO:0000313|EMBL:ELZ31945.1};
OS Halorubrum terrestre JCM 10247.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227486 {ECO:0000313|EMBL:ELZ31945.1, ECO:0000313|Proteomes:UP000011572};
RN [1] {ECO:0000313|EMBL:ELZ31945.1, ECO:0000313|Proteomes:UP000011572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10247 {ECO:0000313|EMBL:ELZ31945.1,
RC ECO:0000313|Proteomes:UP000011572};
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).
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:ELZ31945.1}.
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DR EMBL; AOIW01000054; ELZ31945.1; -; Genomic_DNA.
DR RefSeq; WP_004597636.1; NZ_AOIW01000054.1.
DR AlphaFoldDB; M0D8X4; -.
DR PATRIC; fig|1227486.3.peg.2045; -.
DR Proteomes; UP000011572; 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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..466
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..336
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 544..622
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 476..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 66755 MW; 46238FB61CCC4F52 CRC64;
MFDKVLVANR GEIAVRVMRA CEELGVDTVA VYSDADKHGG HVRYADEAYN VGPARAADSY
LDGEAVVEAA RSAGADAIHP GYGFLAENAD FAARVEAADG ITWVGPESDA MERLGEKTHA
RRVMDDADVP IVPGTTEPVT DVEAVTEFGD EYGYPVAIKA EGGGGGRGMK VVESAEDAEE
ALESAKREGE AYFSNDSVYL ERYLQTPRHV EVQIVADDPD GSVSESDVVH LGERDCSLQR
RHQKVIEEGP SPALSDELRE KIGEAARRGV AAADYTNAGT VEFLVEEDPD RDPSEPLGPE
TNFYFLEVNT RIQVEHTVTE ELTGIDIVKE QLRVASGEGL SVSQGDVALE GHAIEFRINA
ENAANDFQPA NEGSLDTYDP PGGIGVRVDD ALRQGDDLVT DYDSMIAKLI VWAPDREECL
ARSKRALAEY DLEGVVTIVP FHRLMLDDER FVDGTHTTKY LDEELDRELV AEAQEKWGSE
SASAGDDDEE VTEREFTVEV NGKRFDVELE ERGAPAIPVP EGGGGGSGGQ QRPPQAKSDD
GGDDSSVDVA EGGEAIDAEM QGTILSVDVS EGDEVAAGDV VCVLEAMKME NDVVAERGGT
VASVRVGEGD SVDMGDVLIV LE
//
