ID H1V729_COLHI Unreviewed; 1823 AA.
AC H1V729;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:CCF36031.1};
GN ORFNames=CH063_01417 {ECO:0000313|EMBL:CCF36031.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF36031.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CACQ02001802; CCF36031.1; -; Genomic_DNA.
DR STRING; 759273.H1V729; -.
DR EnsemblFungi; CCF36031; CCF36031; CH063_01417.
DR VEuPathDB; FungiDB:CH63R_10383; -.
DR eggNOG; KOG0238; Eukaryota.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_002162_4_0_1; -.
DR Proteomes; UP000007174; 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; 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; 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; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 617..1064
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 736..934
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1745..1821
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1823 AA; 195772 MW; 43F97323FDA6F56D CRC64;
MGSTIQSTFP LTVKEWRETQ EAGDGLARLL SLRESEARLK SNAWITLATP SQIEEQWAHA
ESLRSSGASL PLFGVPFAAK DNIDVASFPT TAACPSFATG PVDKDAAVIA RLKTAGAIVL
GKTNLDQFAT GLVGTRSPYG PVSNSFDPAR VSGGSSSGSS VVVARGVVPF SLGTDTAGSG
RVPAGLNNLV GLKPTRGALS TTRVLPACRS LDCVSIFTLT VDDAETVLAA AEGFDPEDSF
SRARPDTPST VKGHRMAVCD NPPWFGKTEQ AAAYAKALEK AATLGWTLEP VDFSPLFQLA
SLLYEGPWVA ERYAAIKDFI EARESEMDPT VREIILKAKG FNAADLFASE YLRQDLTRQI
QDRFGDFDAI LVPTAPTFPT IEDLAREPIK ENAYLGTYTN FVNFMDWTAL SIPAGFRSDG
LPFGITLISS TWDEPKLLSM AREWLSTGPR LLGATRIERL EARSSDAIAA GEPKTTRLVV
VGAHLTGFPL NKDLTSRGAT LEIATTTSPN YRFYSLNTGG TVKKPGLKRV PSGGSAIQVE
VWSLPTTQLG SFLKTVPSPL GIGSVELADG SWALGFICEP YGLDGATDIT SFGGWRAFVK
SLIPDVPPVG TTSKVSGIRS VLIANRGEIA VRIIRTLHSL GLKAITIHSS ADARSPHVRN
ADVSLPLEGT SVSETYLNGV QIIALAKKAG ADAIIPGYGF LAENADFASA VEAEGLIWVG
PTAEQMRQLG LKHLARDVAI RAGVPVVPGS KHLLKSAEEA LDEAERIQYP VMLKSTAGGG
GIGLKRCDDA ASLVEAFESV QRLAQANFGD AGVFVEHFIE HARHIEVQII GDGCGRVTSA
GERDCSLQRR NQKVIEESPA IFVPPDVRRR MRKAAIDLGS AVKYRNVGTI EFIYDVDTSE
FFFLEVNTRL QVEHPVTESV TGLDLVECMI RVASGNSRHI FVDKPDGFEV KGSSIEVRVY
AESPLQNFRP SPGRLLDVSF PEGVRVDTWV EAGMEMSSSY DPLVAKIIAT GEDRTAAIAK
LADALQKTVI TGVETNLEYA RHIVASEMFR SGTFITTSLN SFAFDSSIVE VVDPGTLTAV
QDFPGRKGLW HVGVPPSGPF DDYSFRLANR LVGNDSRAAG LECTIHGPSL LFHYDAVVAV
TGAFAEVKID NKPAQPNTPL TIQRGQKISI GAATSGYRSY LAVRGGIDVP EIFNSRSTFA
LGKVGGHNGR NLRSGDLLPV GSMVSTAPSA DSGPAIPLPS DPANAHWSIG VVPGQHSAPE
HFTEEGFSTL FVDEWTVHYN SNRIGIRLDG PKPQWARETG GEAGLHPSNI HDSPYSVGSV
SFTGDEAVIL TCDGPSLGGF VVFCVVASAE MWKLGQLRPG DKVKLQPITV DDALFLESAL
EKSIAELTPL AVDVAPLANS PTTPDSNPFL GDIGXAGRRI SVRQAGDNAM LLEFGTEDVF
SLRQSFQIFS FIARHKTHPI PDVLELSPGV RTLHVQYTPK TPPATVLSAL RAHETSLGEA
IPSSISSRTI HLPLAFDDSV SRAAVARYVA TIRATAPWLP SNVDFLQRLN ALDSPADVER
IFLDATFLVL GLGDVFLGSP CAVPLDPRHR LFGTKYNPSR SFTPRGAVGI GGQYMCIYGM
DSPGGYQLVG RTVPIWDDVT ASAVASRGES KPWLFRLFDR ISFYPVSEMD LDAAIDQGRM
TDLVKIEEGS LDLEAYEAWL AANKADIDAT RGLRAGAIRS APFMEELLQP YNPPEAERRG
GAFGEAEDST PGERIKAQMP GRCWKCEVKA GDEVDVGDAL VWIESNKMEI KIGSPIKGKV
VKMLVVEGDI VGPYDDLLIV ETQ
//
