ID A0A136A4D1_9ALTE Unreviewed; 1517 AA.
AC A0A136A4D1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:KXI30093.1};
GN ORFNames=AX660_08830 {ECO:0000313|EMBL:KXI30093.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI30093.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI30093.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI30093.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:KXI30093.1}.
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DR EMBL; LSNE01000003; KXI30093.1; -; Genomic_DNA.
DR RefSeq; WP_068373875.1; NZ_LSNE01000003.1.
DR STRING; 1799789.AX660_08830; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000070299; 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; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50989; COA_CT_CTER; 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}; Reference proteome {ECO:0000313|Proteomes:UP000070299}.
FT DOMAIN 69..292
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT DOMAIN 939..1392
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 1063..1259
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1517 AA; 167694 MW; 439CCED7233AB8D7 CRC64;
MATKERPSNT TRALSADPLF LQAEHLAKDF SLFPAHSKQS LSEEVKGLVS EDVIQANLKN
LASLDVDGYV NKVIQPTQDK NRLGAKRIIA DLKGKIIAEL HIGPFYRAEV ELHFGPRTRR
IGFIAQERTT ANGAWMPEHH LAACKAIRHF ADLSLPIVYL IDTPGADAGE VANSQNQAHS
ISKAIAESAN VDMPTVGIVI GAGYSGGAIP LATANILLSV RDGIFNTIQP QGLQSIARKY
NLSWQECAKS VGVSPEELYS AGCIDGIIDF SPSDKDDRQH NLRRAIISSI EAIEKAAISF
VRESAELKEH YDRSLQRFLT PSVNLLALEN KTSLSIANSP TTHHNIFGSA YRYLRYLTLR
SRIHSIAQDQ YGLLSKVSVP KGDLQIRIKQ EQEHVFQAWL TNPDKLIYDE ELNKLWATFR
NKRSAVSTER NVITRLILGE PKVNYDKARK ALIFNIGWSL YHRWKSNSPN NFAGLIAHLE
SLPTSTTQAP WPELNQLTVL DVVVNDELRE DFIWQCHNIL IFNALYDNVV GSLASISKEA
MMSKSLSRVS VDKLLHKSID NALSSKDSAN DKSKFYKWLR YFMAQSNRAQ LLTRVEQWKS
VGFPQLNDSL FVILTYFFES LLPEYFDSEK DHKKYTGIIN PVRIGRRKDF WNRLTMGYRD
LLIQRVLREE KKLGKMTWEN VISQFFTKFK EIGAEQMSAN LLNFPGFRLS IEDAIEKKIR
PCGLITGLAD FNNKGTKLRV GVAVSNTAFQ AGAFDMASAE KFSSLLIECA KRKLPVICFI
SSGGMQTKEG AAALFSMAVV NDRMTRFIRD NELPVLMFGF GDCTGGAQAS FVTHPLVQTY
YLSGTNMPFA GQMVVPAYLP STATLSNYLS KVSGSMTGLV FNPFSDTLDS QLSEIDPVMP
MPTLKVEDVI SKALSTLVPE EIELDEVIVQ DDPRMLMKPI DKVLVHARGC TAVKLIRKAH
DNNISVVLVA SDPDMTSVPA EMLKDNDKLV CIGGNTSDES YLNAYSVLKV AEYENVDALH
PGIGFLSESP QFAALCVNNG VNFVGPSVHS MTTMGNKSNA IHTSQGQNVP VVPGSHGILS
NAEQAVNVAL EIGYPVLLKA VQGGGGKGIQ VVKRPEDMMN LFQKTATEAA AAFGNGDLYL
EKYVTSLRHI EVQLLRDQFG NTKVLGIRDC SVQRNNQKVI EESGSTMLPE ELKQRVMEYT
RALGNATDYM GAGTVEFIYN LDANEVYFME MNTRLQVEHP VTEATSGIDI VSAQFDIAAG
RSIEALEPIE QGYAMEVRVT AEKAAVDSHG ILQLIPNPGL ITECSMPQGD DIEIISIAAA
GKEISPYYDS LIAQLIIRGK DRADVVAKMY AYLDSVVIKG IATNIPLLKR ILSDATFKDG
VYDTNYLPRL MAELDHQVLI AEMEAAAETA DVDTESLRVG ESNELKVLAH GAGIFYTTPA
QGEAEFVKEG DIVTVEQTLA LMEAMKMFSQ VTLAGFNRQT GVLYPEDQKY RIERILNSNG
QQVSQGDLLF VVSPVEG
//
