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
//