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
//