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Database: UniProt
Entry: G7UTJ7_PSEUP
LinkDB: G7UTJ7_PSEUP
Original site: G7UTJ7_PSEUP 
ID   G7UTJ7_PSEUP            Unreviewed;      1211 AA.
AC   G7UTJ7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:AER54898.1};
GN   OrderedLocusNames=DSC_01225 {ECO:0000313|EMBL:AER54898.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER54898.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER54898.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER54898.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP003093; AER54898.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7UTJ7; -.
DR   STRING; 1045855.DSC_01225; -.
DR   KEGG; psd:DSC_01225; -.
DR   eggNOG; COG0439; Bacteria.
DR   eggNOG; COG1984; Bacteria.
DR   eggNOG; COG2049; Bacteria.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_002162_3_1_6; -.
DR   OMA; TLQMWNR; -.
DR   Proteomes; UP000005870; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
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; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR003778; CT_A_B.
DR   InterPro; IPR003833; CT_C_D.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR014084; Urea_COase.
DR   NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR   NCBIfam; TIGR02712; urea_carbox; 1.
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   Pfam; PF02626; CT_A_B; 1.
DR   Pfam; PF02682; CT_C_D; 1.
DR   SMART; SM00796; AHS1; 1.
DR   SMART; SM00797; AHS2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF160467; PH0987 N-terminal 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; PS50968; BIOTINYL_LIPOYL; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT   DOMAIN          17..460
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          136..333
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1125..1208
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1211 AA;  132543 MW;  956D2915643D2E52 CRC64;
     MIFSSGTTRF EQVVQIMFSK ILIANRGAIA CRIQRTLRRM GIASVAIHTQ ADADSLHVRD
     ADQAICVGQA QAASSYLDIA KVVQAARVSG AQAIHPGYGF LSESLEFAAA CEAAGLVFIG
     PSPEQIRAFG LKHTARELAA SCGVPMLPGS GLLEGLAHAL AQAERIGYPV MLKSTAGGGG
     VGMQRCGDAQ ALQQAYASVQ RLSRNNFGND GLFLEKLVEQ ARHIEVQIFG DGRGRVVALG
     ERDCSLQRRN QKVVEETPAP GLPQEVRERM WATAVRLGET VSYRSAGTVE YIYDDREQRF
     YFLEVNTRLQ VEHGVTEQTT GVDLVEWMVR CAAGESRFLE GFAYAPRGHA IQARLYAEDP
     ARDFQPVAGR ITHSQMPKVG RCDTWIATGT TVSPYYDPML AKLIAHGEDR EQARTRLLAM
     LDETQVAGIE SNLKYLRQVL IAPEFVQARH TTATLAGLAY AASGIEVVEA GTQSTLQDWP
     GRTGYWDVGV PPSGPFDALA LRLGNRLLGN DQGATALEMT LTGAVLRFRS AARIVVAGAD
     MAPTLDGIAI RSWQPYEVQA GATLAFDSVL GAGARCYLCV RGGFDVPPYL GSASTFTLGG
     FGGHGGRALR PGDVLHPAAA AVAEEPACDP ACLPRYTPEW IFRVVYGPHG APDFFTAQDV
     ETFFATAWEV HYNSSRTGVR LIGPRPQWAR TDGGEAGLHP SNLHDNAYAV GAVDFTGDMP
     VILGPDGPSL GGFACPATII KADLWQLGQL RAGDRLRFVA VTVDDADALE RAQQQMIDSL
     RVVPAPAGAR RALPASPVLA EDERDGIRVV YRPSGEDNVL VEYGQMVLDL DLRFRVHALM
     SWLQRQRIGD LLELTPGVRS LQVHYDNQRL PQREVLALLR AAERQLPAVA EMEVPTRIVH
     LPISWDDAAC RRAVEKYMQL VRHDAPWCPD NLEFIRRING LDDVEEVRRI FFDASYLVMG
     LGDVYLGAPV ATPLDPRHRL VTTKYNPART WTPENAVGIG GAYLCVYGME GPGGYQFVGR
     TLQMWNAWHR TAEFAEGKPW LLRFFDQLRF YPVSHEELLQ IREDFPRGRY RLRIEEQTFR
     LRDYHAFLAA NGDSIAAFKQ RQQAAFEAER QRWAEAGYDE VVGVEETVEA PLLQLAGNER
     AIAGTVPGSV WKVLVQPGQR VDAGQPVVVL ESMKMEIAVE SRYGGRVSSV QCAAGQTIAP
     GQPLVIVAVE P
//
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