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Database: UniProt
Entry: A0A0N8KB20_9ALTE
LinkDB: A0A0N8KB20_9ALTE
Original site: A0A0N8KB20_9ALTE 
ID   A0A0N8KB20_9ALTE        Unreviewed;      1092 AA.
AC   A0A0N8KB20;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUN-2019, entry version 14.
DE   SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:KPQ01714.1};
GN   ORFNames=HLUCCO03_11425 {ECO:0000313|EMBL:KPQ01714.1};
OS   Marinobacter sp. HL-58.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=1479237 {ECO:0000313|EMBL:KPQ01714.1, ECO:0000313|Proteomes:UP000050516};
RN   [1] {ECO:0000313|EMBL:KPQ01714.1, ECO:0000313|Proteomes:UP000050516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-58 {ECO:0000313|EMBL:KPQ01714.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPQ01714.1}.
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DR   EMBL; LIHP01000004; KPQ01714.1; -; Genomic_DNA.
DR   RefSeq; WP_027831894.1; NZ_JMLY01000001.1.
DR   STRING; 1479237.JMLY01000001_gene2219; -.
DR   EnsemblBacteria; KPQ01714; KPQ01714; HLUCCO03_11425.
DR   PATRIC; fig|1479237.4.peg.3888; -.
DR   Proteomes; UP000050516; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   SUPFAM; SSF52440; SSF52440; 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; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050516};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Pyruvate {ECO:0000313|EMBL:KPQ01714.1}.
FT   DOMAIN        2    452       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    318       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      475    556       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      574    842       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000259|PROSITE:PS50980}.
FT   DOMAIN      836   1083       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000259|PROSITE:PS50989}.
FT   REGION      470    492       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0N8KB20}.
SQ   SEQUENCE   1092 AA;  117081 MW;  D97936B0EFF9A0E0 CRC64;
     MPFQRLLIAN RGEIAIRVAR AASELDIPTV AVFARDDSQS LHVRKADAAA ALDKSGAAAY
     LDGEQLVRIA KEYGCDAIHP GYGFLSESAE FARLCETAGI YFIGPSAAAL DVFGDKASAR
     QMARKHGVPL IHGTNEPTSL ASARVFMESL GEHGQVMLKA IAGGGGRGMR PVKSVDELES
     AFHRCRSEAS AAFGNGDLYI EQLISDARHI EVQIIGDGST ATHLWERECT LQRRNQKVVE
     VAPAPDLDPE LRSRLLADAG MLACAVGYRG LCTIEFLVDT KTGQYVFMEA NPRLQVEHTI
     TEAITGLDLV QLQIRVAAGM SLVDLGLASA PEPRGRAMQL RINLETMAKD GSTRPAGGRI
     DTYEPPSGPG VRVDGYGYSG YTTSPAFDSL LAKLVVHAEG DFPALLRRAY RALCEFRLEG
     VPSNIAFLQN LLRHPRVQAN DVSTRFIDTH IKELVPDDPA LHPNLYFSET ATTESSEDTT
     PEGPDGAEPI TSPARGVVVS IDVEPGQAVV EGQPVAVLEA MKMEFVIKAG ASGHVISITA
     SPGDTIGEQH PLMFIEPTAV SAGEVDTEES VDIEHIRADL QQVLDLHKQL GDDSRPDAVA
     KRRKTGQRTA RENLADLLDD GSFREYGALA LAAQRTRRSP EELRDLSPAD GLVAGIGTVN
     GEYFSPEAAR CMAMSYDYTV FAGTQGVMNH KKTDRMLELA EKQRLPLVFF TEGGGGRPGD
     VDWVGVAGLD CTTFLRMARL SGKVPLVGIA SGRCFAGNAA LLGCCDVIIA TANATIGMAG
     PAMIEGGGLG RFMPEEVGPV SVQSHNGVVD IVARDEAEAT GIARKYLACF QGDLPAGETG
     DQRLLRHLIP ENRLRVYDIR EVIDALADRG SVIELRKQFA PGMITALVRI RGKAFGLIAN
     NPMHLGGAID AAAADKAARF MQLCDAHGLP LLSLCDTPGF MVGPEAEKQA TVRHVSRMFV
     TGASISVPFF TVVLRKGYGL GAQAMAAGSF HAPMFTIGWP SSEFGAMGLE GAVRLGFAKE
     LAAVENQDER KALFDKLVGQ LYERGKGVSM TSFLEIDAVI DPAETRDWLI RGLASVDPES
     LRSGGRPMVD TW
//
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