ID A3GG31_PICST Unreviewed; 1822 AA.
AC A3GG31;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 2.
DT 24-JAN-2024, entry version 110.
DE SubName: Full=Urea amidolyase {ECO:0000313|EMBL:EAZ63450.2};
DE EC=3.5.1.54 {ECO:0000313|EMBL:EAZ63450.2};
DE EC=6.3.4.6 {ECO:0000313|EMBL:EAZ63450.2};
DE EC=6.4.1.4 {ECO:0000313|EMBL:EAZ63450.2};
GN Name=DUR1 {ECO:0000313|EMBL:EAZ63450.2};
GN ORFNames=PICST_28452 {ECO:0000313|EMBL:EAZ63450.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:EAZ63450.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:EAZ63450.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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:EAZ63450.2}.
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DR EMBL; AAVQ01000001; EAZ63450.2; -; Genomic_DNA.
DR RefSeq; XP_001387473.2; XM_001387436.1.
DR STRING; 322104.A3GG31; -.
DR GeneID; 4851230; -.
DR KEGG; pic:PICST_28452; -.
DR eggNOG; KOG0238; Eukaryota.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_002162_4_1_1; -.
DR InParanoid; A3GG31; -.
DR OMA; GGMYMCI; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0004039; F:allophanate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; 3.90.1300.10; Amidase signature (AS) 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; 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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAZ63450.2};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAZ63450.2};
KW Lyase {ECO:0000313|EMBL:EAZ63450.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 625..1067
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 744..941
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1746..1822
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1822 AA; 200619 MW; 38937441941357B3 CRC64;
MSYIGWSVQD WIQFHYQSTP NESFALLQEL LGDQNKAPED PAWISLATLD NLKHQWHFLQ
SKSNKLDLPL YGVPVAIKDN IDVKGFETTA ACPSFAYSPE DDATTVKLLR NAGAIVIGKT
NLDQFATGLV GTRSPYGITP NTFNKDYVSG GSSAGSASVV ARGIVPISLG TDTAGSGRVP
AALNNIIGLK PTKGVFSCAG VVPACKSLDC VSIFSLNLQD AQLVFNIMAQ EDALNDEYSR
PLPANPLIKF PATPKIAVPT NLLWFDETEN PKIYNKAVDH FKENVGAELV PLNIDLLLDL
AKCLYEGPWV SERFAATKDF FATNPPAADL DPTVTQIIKG GEKHSAATAF EYEYKRQGII
QKVSKLLEGI DAIIVPTAPL NPTIAEVTKE PIKVNANQGT YTNFVNLADM SALAIPAGFR
SDGLPFGITL LSHKFNDYAL LDLASRYLKG VDSTEKRFYG CLKDKPVSSL GDELLPNIPG
FDPESQIKLA VVGAHLKGFQ LHWQLEKVRA NLIESTTTSG NYKLYALPKT GPVAKPGLRR
VTENGTKIAL EVYAVPKETF GDFIAMVPEP LGIGSVELTS GEWVKSFICE EVGYNAPGTT
DVSSFGGWKN YHEHLAQEAK AQKKPFKSVL VANRGEIAVR IIKTLKRLNI KSIAVYSDPD
KYAKHVLIAD AAVPLHGTSA AETYIAVEKI IQAAKDTGAE AIIPGYGFLS ENADFSDRCG
KEGIVFVGPS GDAIRKLGLK HSAREIAEKA GVPLVPGSGL VKDALEAKEI AAKLEYPVMV
KSTAGGGGIG LQKVDSEKDI ERVFETVQHQ GKSYFGDAGV FLERFVEDAR HVEVQMFGDG
KGRAIALGER DCSLQRRNQK VIEETPAPNL PEATRQKMRD AAESLGASMN YKCAGTVEFI
YDEKRDEFYF LEVNARLQVE HPITEMVTGL DLVEWMLYIA ADDPPDFSQK IEVTGASMEA
RLYAENPVKD FMPSPGQLTE VKFPEWARVD GWVEKGTVIS AEYDPTLAKI IVHGKDRNDA
LKKLRQALDE TVVFGCITNI DYLRSIINSS MFAEAKVATK VLDSYDYRPT AFEIISPGAY
TTVQDYPGRK GYWHIGVPPS GCMDEYSFRV ANRIVGNDKV APGIEITLNG PKLLFHHDAV
IAVTGGAVEI DINGYKVEQW APLHVKRGDK VSIGKLTTGC RAYLAIRGGI DVTEYLGSRS
TFALGNLGGY NGRVLKLGDV LFLGQPEISS CTLPAPISEP SNIAPSLIPN YDNKVWQVGV
TCGPHGSPDF FKPEAIETFF KDTWKVHYNS NRFGVRLIGP KPVWARPDGG DAGLHPSNTH
DYVYSLGAIN FTGDEPVILT CDGPSLGGFV CAAVVVESEM WKIGQVKPGE QIQFIPISYE
TSIELKNQQD KIIENLTGDL PSFDGKAIKP ENPVLFEFSA SSNAPKVVYR QAGDRYILVE
YGENCMDLNT SYRIQRLIEM VEEHKTRGIV EMSQGVRSVL IEFNREVTQD ELLKTLISYE
KEIFFINKWE VKSRIIKLPM AFEDKKTLDA VKRYSETIRS EAPWLPNNVD FIANINGITR
EEVRDLAYTA RFMVLGLGDV FLGAPCAVPL DPRQRLLGTK YNPSRTYTPN GTVGIGGSYM
CIYTMESPGG YQLIGRTVPI WDKLTLASHS GDKPWLLRPF DQVEFYPVSE EEIDKFSEEM
NAGKFKVDII ETVFKHGKYL EWIQEHSDSI AEFQKNQGGE KLEEFNRLIQ ISNSELEKSG
TKIVEDESYD DTHELVYSEY SGRFWKSLVE TGDEVKAGRA LIVVEAMKTE MVVSAPRDGK
VVKIYHKNGD MVDAGDLVVV LA
//
