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Database: UniProt
Entry: K0KPJ2_WICCF
LinkDB: K0KPJ2_WICCF
Original site: K0KPJ2_WICCF 
ID   K0KPJ2_WICCF            Unreviewed;      1828 AA.
AC   K0KPJ2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 62.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:CCH43078.1};
DE            EC=6.3.4.6 {ECO:0000313|EMBL:CCH43078.1};
GN   ORFNames=BN7_2625 {ECO:0000313|EMBL:CCH43078.1};
OS   Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS   3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH43078.1, ECO:0000313|Proteomes:UP000009328};
RN   [1] {ECO:0000313|EMBL:CCH43078.1, ECO:0000313|Proteomes:UP000009328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC   Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX   PubMed=23193139; DOI=10.1128/EC.00258-12;
RA   Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA   Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA   Tauch A., Kohler T., Brinkrolf K.;
RT   "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL   Eukaryot. Cell 11:1582-1583(2012).
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:CCH43078.1}.
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DR   EMBL; CAIF01000068; CCH43078.1; -; Genomic_DNA.
DR   STRING; 1206466.K0KPJ2; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_002162_4_1_1; -.
DR   InParanoid; K0KPJ2; -.
DR   Proteomes; UP000009328; 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:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 1.20.58.1700; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 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   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR   Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR   InterPro; IPR014085; Allophanate_hydrolase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
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; 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; TIGR02713; allophanate_hyd; 1.
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; PF01425; Amidase; 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; SSF75304; Amidase signature (AS) enzymes; 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; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCH43078.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000009328}.
FT   DOMAIN          619..1070
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          738..943
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1750..1828
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1828 AA;  201648 MW;  E434415E965E48AB CRC64;
     MSYIGWTAKD WIDFHKNSTP DDSLDQLLQL LKSQNSAPQD PAWISLASEE NIKHQWQILQ
     SKLHKEELKL YGVPIAVKDN IDAKDFETTA ACPSFAYTPE KDAFVVKLLK DQGAIVIGKT
     NLDQFATGLV GVRSPYGKTP CAFSDKHVSG GSSAGSANVV ARGIVPIALG TDTAGSGRVP
     AALNNLIGLK PSLGVFSTNG VVPACKSLDA PSIFSLNLSD AQLCFSIMAK PDPLNDEYSR
     SLPSNPLQSF GKTPKIAIPE NLPWYGETEN PKLYNKAIEN LKATGAEIVK IDFTDLLDLA
     KCLYEGPWVA ERYAATKDFL STNPPEDSLD PTVIGIIKTA TKFSAADAFK YEYKRQGILQ
     KVRQLLKGID VLAVPTCPLN PTFDDLAKEP VVVNSYQGTW TNFVNLADMA ALALPAGFRP
     DGLPNGVTLI AQKFTDYALL DLANKYLKIA FTPEQRPLGA TKSKSLLGDE LSVPKPDLSQ
     SIKLAVVGAH LKGMDLHWQL EKVNATLIKS IKTSKHYKLY ALPKVGPVAK PGLRRVTESG
     EKIQLEVYSV PLENFGTFIS MVPQPLGIGS VELEDGEWVK SFICEEYGYL QKGTTDITSF
     GGWKNYIQET SKSSPAKKPF NTVLVANRGE IAVRIIKTLK KMGITAVSIY SDPDQYSQHV
     LDSDIALPLH GDSAAETYIN IEKVIKAAKD SKAEAIIPGY GFLSENADFA DRCEKEGIVF
     VGPSGDSIRK LGLKHSAREI AEKAGVPLVP GSGLISDVSE AVEFAKKLGL SNDPETSVKV
     MLKSTAGGGG IGLQKVDLLD DLPNSFETVQ HQGKAYFGDA GVFLERFVEN ARHVEIQMFG
     DGFGHAIALG ERDCSLQRRN QKIIEETPAP NLPESTRQKM RKAAEQLGSS MNYKCAGTVE
     FIYEEKRDEF FFLEVNARLQ VEHPITEAVT GLDLVEWMLK IAANDSPDFS KQVITVTGAS
     MEARLYAENP VKDFRPSPGQ LTDVSFPEWA RVDTWVKKGT VVSAEYDPTL AKIIVHGKDR
     AEALKLLQKA LDETTVYGCI TNLDYLRSVG NSKMFEEAKM HTKILDSYDY RANAFEILSP
     GAYTTVQDYP GRVGYWRIGV PPSGPMDNYS FRLANKIVGN ANASPAIEIT LNGPTIQFHT
     DAIIAITGGE VESKINNDVV KQWEPLHIKR GDKLAIGKLT KGSRAYLAIR NGIDVSEYLG
     SRSTFALGNM GGYNGRVLKL GDVLFVGQPY LDGNTLPAPE SEPVSLPKEL IPAFETKEWT
     VGVTCGPHGS PDYFKPESVD EFFSEQWKVH YNSNRFGVRL IGPKPKWARA DGGEAGLHPS
     NQHDYVYSLG AINFTGDEPV ILTCDGPSLG GFVCQAVVAD AEMWKIGQVK PGDLIKFVPV
     SYNAARSLKI TQDETIESFK GSYPSLSGDL VLSKPENPVL ATFKAFDNSP LATYRQAGDR
     YILLEYGELM DLNISYRINR LIEMVDLHHT VGIIEMSQGV RSVLIEYDGY LIDQSSLIET
     LIAYERELIF ENKWKIKSKV FKLPMAFEDK KTLDCVTRYQ ETIRSEAPWL PNNVDFIADV
     NDISREDVRD MLYSARYLVL GLGDVFLGAP CATPLDPRQR LLGSKYNPSR TYTANGVVGI
     GGMYMCIYAM DSPGGYQLVG RTIPIWDKLK LGEHSSEHPW LLTPFDQVEF YPVSEEELDK
     FTEDAKHGQF KVDYEESVFD HEEYLRWIDK NIESIREFEK NQKGEKAAEF AKLIQVANED
     LEKNGANKQE AEEQYPEDAE LVYSEYNGRF WKPLVKVGDT VKEGDGLVVV EAMKTEMVVN
     ATKSGKVLKI LHVNGDMVES GDLVVVIN
//
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