ID A0A0D2FD73_9EURO Unreviewed; 1245 AA.
AC A0A0D2FD73;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:KIW65978.1};
GN ORFNames=PV04_08191 {ECO:0000313|EMBL:KIW65978.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW65978.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW65978.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW65978.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KN846960; KIW65978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2FD73; -.
DR STRING; 5601.A0A0D2FD73; -.
DR HOGENOM; CLU_002162_0_1_1; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000054266; 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; 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}.
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 1159..1239
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 1098..1139
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1245 AA; 136816 MW; 78C043144DE06251 CRC64;
MQKLKTLLVA NRGEIAVRIC KTARELGIKT ISIYTGADAA SAHVGAADEA VLLSGPDAKG
YIDGEQIVGI AKSKGADAVI PGYGFLSENT DFARQVSEAG MVFVGPSSKC IDDFGIKHTA
RELAAKADVP IVPGTRGLVQ SEDEAVEEAK KLGFPVMLKA TAGGGGMGLL TCNNESEVRQ
SFKTVQSRGE TLFKNSGLFI EKFFPSSHHI EVQVFGNGLG QAIHFGEREC SIQRRHQKVV
EECPSPFVVK HPELRAKLGA AAVRLAESIS YGSAGTIEYL VDDESGDFFF LEMNTRLQVE
HGITEMCYGV DLVELMLKQA DAQLSGTGGL DGEYLRNLQP NGPSGAAIEV RVYAENPAKD
YAPSPGTLQH VSWKEVPGCR IDGWIHTGTK VTSFYDPLLA KVMVHAAERA EAIRLMAEML
DGSKIFGPPT NLDFLASILQ DETFKSGRTM TKFLDSFKYQ PAAIYVLQGG AYTLVEDWPG
RPTIGKGFSH SGPMDPLAFR IANALVGNPP GKEGMEITLS GPDLKFLGAA IVAVCGAPME
VKLDGRDVPM WTRLKIEAGQ RLTVGKTTGG GCRSYLAIHG GLPSIATWFG SKSTAPMTGV
GGYQGRALAA GDLLAITKDL PEISGELKLP DNLIPSYPTE WDLFAMPGPY DEGFITSASI
EEFYSTTWTI SHNAARGGIR LIGPKPKWAR PDGGEGGAHP SNVIEYGYPI GTVNWTGDDP
CLFPIDAPDF GGFVSATTII KADYWRMGQM KAGNKLRFQR VSYQDAMAKR KEVETFLGAV
HECCNGMAKF EDVAPLKYDS FPSSVDNKGW ERAIIHQIQE DSGKHQPLVS YRQGADDFIL
IDYGHGSFDL NYRCRAVALY RKLRESTGEI SFSNGALHTG MACGNSLMLY YDSTKVARPT
MMDYLLKLET ELGDLSEAKF PSRKYKFPIT FESKRQKESL QRYMETQRPY ASYLPDPMEF
VAKNNAFSMQ QLRDIYTKSS LMVVAVGFFV ALPIALPVDP RQRIQCPKMN PSRVHTPEGQ
VGWGGSCMAL YNVESPGGYM NTGLSIPGAD ILGFKKGYSS ERPWLFEDFD QITFYEVTED
EYEAMMAVFR SGRYEYQYED TEFDMKEHNK LLRDTKDEVE QIRAKQRQAQ AEMDKLEKEL
LEKWSKEKEA GQISMDTVEE LLHDPDIIAV EAPLNANVWK VEVKEGDTVK LEQVVSILEA
MKLEIPVKAE QSMEGATVEK LLVKPNDVVS AGKTLMLLRR PGTKA
//
