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Database: UniProt
Entry: U2BCZ8_9PSED
LinkDB: U2BCZ8_9PSED
Original site: U2BCZ8_9PSED 
ID   U2BCZ8_9PSED            Unreviewed;      1213 AA.
AC   U2BCZ8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:ERI53091.1};
GN   ORFNames=N878_00525 {ECO:0000313|EMBL:ERI53091.1};
OS   Pseudomonas sp. EGD-AK9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI53091.1, ECO:0000313|Proteomes:UP000016488};
RN   [1] {ECO:0000313|EMBL:ERI53091.1, ECO:0000313|Proteomes:UP000016488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA   Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA   Purohit H.J.;
RT   "Indian agricultural soil isolates capable of pesticide degradation.";
RL   Submitted (AUG-2013) 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:ERI53091.1}.
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DR   EMBL; AVOF01000129; ERI53091.1; -; Genomic_DNA.
DR   RefSeq; WP_021442973.1; NZ_AVOF01000129.1.
DR   AlphaFoldDB; U2BCZ8; -.
DR   PATRIC; fig|1386078.3.peg.1352; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000016488; Unassembled WGS sequence.
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}.
FT   DOMAIN          1..450
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..317
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1135..1211
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          771..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1213 AA;  131211 MW;  0689369FC9878F68 CRC64;
     MFDKLLIANR GAIACRILRT LRELNVSGVA VYAEADAASL HIQQADEAFC LGDGPAAQTY
     LVVEKILDVA KRSGAKAIHP GYGFLSENAA FAEACEAAGI AFVGPTPEQL RVFGLKHTAR
     ALAKQHGVPM LEGTELLENL DAALAAGEQV GYPVMLKSTA GGGGIGMRVC RSAAELSEAF
     EAVKRLGQNN FSDSGVFIEK YIQRARHLEV QVFGDGQGEV LAFGVRDCSV QRRNQKVLEE
     TPAPNLPAGM ADELCAAAIK LAKAVSYRSA GTVEFVYDSE AERFYFLEVN TRLQVEHGVT
     EQVWGVDLVR WMIELAAGDL PPLSELAKTL EPSGHAIQAR LYAEDPGRDF QPSPGLLTAV
     ALPPADGKAL RIDTWVEAGC EIPPYFDPMI AKLITWAPTR EEASAALDKA LADSVLYGVE
     CNRDYLRQIL SDAPFASGHP WTRCLENLVY QPSTFEVLSA GTQTSVQDFP GRLGYWAVGV
     PPSGPMDSRA LRLGNRLLGN AEGAAGLEIT MSGPLLRFNT DAVVAVTGAE IPLSVDGVEQ
     PMNTALLIKA GTTLALGTIA GSGARSYLTL RGGLQVPEYL GSKSTFTLGQ FGGHGGRALR
     AGDVLHLLPL TDTGSGAQLP AELCPTLPAV RELRVIYGPH GAPEYFSERY IDRFLATDWE
     VHFNSSRTGV RLIGPKPEWV RDSGGEAGLH PSNIHDNPYA IGAVDFTGDM PVILGPDGPS
     LGGFVCLVTI IEADLWQLGQ LKAGDKVRFV PVDIAAARAL AQGNARECTT LSRSGFSRDT
     DGTPIADKSA PTDSTELSSP IVLDLGEGDT RLVARLSGDT HLLLEIGAPE LDLVLRFRGH
     ALMQALEAKQ LDGVIDLTPG IRSLQVHYQP ETLSLARLLA AVIGEWDAVC NATDLRVPSR
     IVHLPLSWDD PACQLAIEKY MTTVRKDAPW CPSNLEFIRR INDLPNLDEV YKTVFDASYL
     VMGLGDVYLG APVATPLDPR HRLVTTKYNP ARTWTAENSV GIGGAYMCVY GMEGPGGYQF
     VGRTLQMWNR YREVTAFHGK PWLLRFFDQI RFYPVSAEEL LQIRRDFPLG RYPLRIEHSE
     LALADYQQFL ADEAAGIDAF RRQQRAAFAA ERQRWIESGQ AHFEVEEVAA ELGEDAPLGA
     GQHGIDSHIA GNLWQVQVAE GARVEAGDVL VILESMKMEI PLTAPVAGTV REVRVQPGSP
     VRAGQRVVVL EQA
//
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