ID A0A1R3RM18_ASPC5 Unreviewed; 1237 AA.
AC A0A1R3RM18;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=Urea carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPCADRAFT_170159 {ECO:0000313|EMBL:OOF95499.1};
OS Aspergillus carbonarius (strain ITEM 5010).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF95499.1, ECO:0000313|Proteomes:UP000188318};
RN [1] {ECO:0000313|Proteomes:UP000188318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KV907500; OOF95499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3RM18; -.
DR STRING; 602072.A0A1R3RM18; -.
DR VEuPathDB; FungiDB:ASPCADRAFT_170159; -.
DR OMA; TLQMWNR; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000188318; 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; 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; 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 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000188318}.
FT DOMAIN 3..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1154..1234
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 1107..1134
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1237 AA; 135254 MW; 08758B06D5227368 CRC64;
MESLKTLLVA NRGEIAVRIL KTAKNLSLRT IVVYTEPDAA STHVHLADEA VLLTGAPSKA
YIDGDQIIQI AKRNNADAII PGYGFLSENA DFARAVASSG IAFVGPSPES IEAFGLKHTA
RDLATKAGVP IVPGSQGLVK SEDEAVAIAK ELGFPVMLKA TAGGGGMGLL TCNTEKEVRD
SFLTVKSRGE ALFKNAGIFI ERYYPSSHHI EVQVFGNGDG KAIYIGEREC SIQRRHQKVI
EECPSPFVTR NPGLREKLGD AAVRLAESIR YGSAGTIEYL VDDETGAFFF LEMNTRLQVE
HGITELCYGI DLVELMLKQA DAQLSGKNGV DAAYLGKIPV HAPSGAAIEA RVYAENPAKD
FAPCPGTLQT VEWKDLPGSR IDTWIYRGVK VSANYDPLLA KVMYHSPSRE QTIEGMRTIL
TESRICGPPT NLEFLAEVLA NDKFVAGKTL TRFLNDFKYQ LSAIDVISGG AYTLIEDWPG
RPTLGRGFCH SGPMDPTAFR IANALVGNPI GLEALEITLS GPELRFLGPA IISLCGAPIE
ARLDDTPFPM WSRVKVSAGQ RLRIGKTTGN GCRAYLGVFG GFLNVAEWFG SKSTTPGVGV
GGYQGRQLAS GDLLSITSQV PEISGDLRLP QQLIPQYPDH WEIMAMPGPY DEGYLVPESI
DMLYSTNWKV SHNAARGGVR LLGPKPTWAR TDGGEGGAHP SNLIEYGYAI GSLNWTGDDP
VIFPVDAPDL GGFVSSHTIC KADLWKLGQV KAGDTLKYRA TSLEDALSSR KEIERFIHEV
AQGCQKGDLS GISPVNNDLA AELTAEDRGS GVIHQIQASG SQPLVSYRQA GDDYLLIDYG
TGAFDLNHRC RVTALKKALT EGTGNITFST GLTSMLGCGN SLMLYYDGTR IPQQELLAYL
CDIETKLGDL SQAKFPSRLF KLPLSFESQR QKDALTRYME TQRSYASYLP DNMDFVAKNN
AFSREEFERI YLTASFMVVA VGFFTALPLS TPVDPRHRMN CPKMNPSRVY TPAGSVSWGG
SCMALYNVDS PGGYQMTGMT IPGVDILGSK KGYEANRPWL FEDFDQITFY RVSEDEYEKQ
LALFNSGRYE YQWEEVVFDM AEHNKLLHDT KDEVAAIRSK QRQAQAEMDK LEADLLDRWA
KEKAERGIPI DTIENLLKDP EITPIEAPLN ANIWKVEVKE GDKLDANQLV VILEAMKLEI
AVRTESLASG STVEKILVQP GDSIEAGKPL VLVRTQK
//
