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Database: UniProt
Entry: A0A2H3JF43_WOLCO
LinkDB: A0A2H3JF43_WOLCO
Original site: A0A2H3JF43_WOLCO 
ID   A0A2H3JF43_WOLCO        Unreviewed;      1248 AA.
AC   A0A2H3JF43;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   SubName: Full=Urea amidolyase {ECO:0000313|EMBL:PCH34617.1};
GN   ORFNames=WOLCODRAFT_133538 {ECO:0000313|EMBL:PCH34617.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH34617.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH34617.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH34617.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; KB467832; PCH34617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3JF43; -.
DR   STRING; 742152.A0A2H3JF43; -.
DR   OMA; TLQMWNR; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000218811; 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:0016829; F:lyase 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; 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   NCBIfam; TIGR00724; urea_amlyse_rel; 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; PS00188; BIOTIN; 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};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lyase {ECO:0000313|EMBL:PCH34617.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000218811}.
FT   DOMAIN          3..471
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          127..328
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   1248 AA;  136375 MW;  71ADE759E15333F7 CRC64;
     MDVGHKLLVA NRGEIAVRVL RTAKRLGLRT VAIYTRTDAT SPHVVLADES VALNPDDTDS
     VSNARGYLDA ETIVAICRAH RVTLVHPGYG FLSENAHFAS LLAEAGVTFL GPKNETIQAM
     GLKHEARILA TAVDVPLVPG SQGLIENVED AVLLADRIGY PVMLKSTAGG GGMGLVMCQN
     ANELRVKFVA TQERATTLFK NGGVFLERYY PSARHVEVQV FGNGLGHAIH IGERECSVQR
     RHQKVIEESP SPFMIGYPDV GQRMCTAAIR LCQHINYASA GTVEFLVDDA TGDFFFLEMN
     TRLQVEHPVT EATNPGLDIV ELMIRQGVAE RNTELGGLAA NQLSQEPYNI PSHKRPLHAI
     EARVYCENPA AQFKPSPGVL QKVEFMQAEW LRVETWVETG TTVTPYFDPL VCKLIVTGTN
     RQQAIDRLEV ALAGCKVHGP PNNMAYLRAI CQSEVFRAGN TMTTYLDTFN FVPRTMDVLS
     GGLETTVQDY PGRRIGMGIP RGGPMDSLAF RAANILVGND PGTEALEITL VGCKVLFHVP
     TVIAVAGAPV RVTVNGQEAQ TWSSILVPAG GKVAVGTINS VGFRAYLAVR GGFPEIPVYL
     GSKSTSIGLG GYQGRALTAG DHLALGDCGP VQDEQPTTVP DSLRPSYPSD WVIYCLQGPH
     CDEEFVTAEG IEKFCSTKWK VSTSSNRMGI RLEGPSILWA RRTGGEGGSH PSNIHDNGYA
     FGTINVNGDT PVILTNDGPD MGGYTCLCTI ATEELWKIGQ LRPGSTVQFR RISPAQSVSM
     VALRERYFTQ LAEAARSSAL KSVPEKADLF DQVFEDCSQD PKIHTIVPLE GSMRPKVVFR
     QAGDSAILVE FGELQLDFML RARIHAFETE LRRRSVQGIW SLAPCIRSTM IHYDPCSISQ
     AALLSVLVDV ETSLPDNLEE TVFPARRITF PIVLDDRWNR EALQRYMRSI RDEAAYLPSN
     IEYLARNNGL AGGVEEALKA LISSDWLVFG VGFYMACPFL IPIDPRCRLV GQKMNPSRTF
     TPRGAVGIAG LVAAIYPIES PGGYQLFGRS LSPWQTWGKG PDFDLEKPWL LQPFDQVAFQ
     PVTEEEYIQL ESQLDAGRYA FKIEPSNFSI SEYSSFIRGI SEQVKQFKER QARGVESEEA
     RETELFAKWV ERKAEAHSTV HETANSNDAF AVGDGIVSSM SASIWRIKCK PGDVISSAGD
     VVVILEAMKT EINIEAGEEN IGRKVMGFGK GVKEGAAVNA GDVLVVLQ
//
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